G. Lipari and A. Szabo, Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results, Journal of the American Chemical Society, vol.104, issue.17, pp.4559-4570, 1982.
DOI : 10.1021/ja00381a010

D. Marion and K. Wüthrich, Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1, 1983.

J. L. Martin, Thioredoxin ???a fold for all reasons, Structure, vol.3, issue.3, pp.245-50, 1995.
DOI : 10.1016/S0969-2126(01)00154-X

J. L. Martin, J. C. Bardwell, and J. Kuriyan, Crystal structure of the DsbA protein required for disulphide bond formation in vivo, Nature, vol.365, issue.6445, pp.464-472, 1993.
DOI : 10.1038/365464a0

J. E. Masse and R. Keller, AutoLink: Automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic, Journal of Magnetic Resonance, vol.174, issue.1, pp.133-51, 2005.
DOI : 10.1016/j.jmr.2005.01.017

D. A. Mavridou, J. M. Stevens, S. J. Ferguson, and C. Redfield, Active-site Properties of the Oxidized and Reduced C-terminal Domain of DsbD Obtained by NMR Spectroscopy, Journal of Molecular Biology, vol.370, issue.4, pp.643-58, 2007.
DOI : 10.1016/j.jmb.2007.04.038

A. A. Mccarthy, P. W. Haebel, A. Torronen, V. Rybin, E. N. Baker et al., Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli, Nat Struct Biol, vol.7, pp.196-205, 2000.

S. Meiboom and D. Gill, Modified Spin???Echo Method for Measuring Nuclear Relaxation Times, Review of Scientific Instruments, vol.233, issue.8, pp.688-691, 1958.
DOI : 10.1103/RevModPhys.26.167

J. Messens and J. F. Collet, Pathways of disulfide bond formation in Escherichia coli, The International Journal of Biochemistry & Cell Biology, vol.38, issue.7, pp.1050-62, 2006.
DOI : 10.1016/j.biocel.2005.12.011

J. Messens and S. Silver, Arsenate Reduction: Thiol Cascade Chemistry with Convergent Evolution, Journal of Molecular Biology, vol.362, issue.1, pp.1-17, 2006.
DOI : 10.1016/j.jmb.2006.07.002

D. Missiakas, F. Schwager, and S. Raina, Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli, Embo J, vol.14, pp.3415-3439, 1995.

G. A. Mueller, A. M. Smith, M. D. Chapman, G. S. Rule, and D. C. Benjamin, Hydrogen Exchange Nuclear Magnetic Resonance Spectroscopy Mapping of Antibody Epitopes on the House Dust Mite Allergen Der p 2, Journal of Biological Chemistry, vol.4, issue.12, pp.9359-65, 2001.
DOI : 10.1111/j.1365-2222.1996.tb00615.x

H. Nakamoto and J. C. Bardwell, Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1694, issue.1-3, 2004.
DOI : 10.1016/j.bbamcr.2004.02.012

H. Nakamura, M. Matsuda, K. Furuke, Y. Kitaoka, S. Iwata et al., Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide, Immunology Letters, vol.42, issue.1-2, pp.75-80, 1994.
DOI : 10.1016/0165-2478(94)90038-8

T. Nakanishi, M. Miyazawa, M. Sakakura, H. Terasawa, H. Takahashi et al., Determination of the Interface of a Large Protein Complex by Transferred Cross-saturation Measurements, Journal of Molecular Biology, vol.318, issue.2, pp.245-254, 2002.
DOI : 10.1016/S0022-2836(02)00018-9

L. E. Netto and E. R. Stadtman, The Iron-Catalyzed Oxidation of Dithiothreitol Is a Biphasic Process: Hydrogen Peroxide Is Involved in the Initiation of a Free Radical Chain of Reactions, Archives of Biochemistry and Biophysics, vol.333, issue.1, pp.233-275, 1996.
DOI : 10.1006/abbi.1996.0386

D. Nietlispach, H. R. Mott, K. M. Stott, P. R. Nielsen, A. Thiru et al., Structure Determination of Protein Complexes by NMR, Methods Mol Biol, vol.278, pp.255-88, 2004.
DOI : 10.1385/1-59259-809-9:255

J. E. Oblong, E. L. Chantler, A. Gallegos, D. L. Kirkpatrick, T. Chen et al., Reversible inhibition of human thioredoxin reductase activity by cytotoxic alkyl 2-imidazolyl disulfide analogues, Cancer Chemotherapy and Pharmacology, vol.87, issue.5, pp.434-438, 1994.
DOI : 10.1007/BF00685570

F. Osterberg, G. M. Morris, M. F. Sanner, A. J. Olson, and D. S. Goodsell, Automated docking to multiple target structures: Incorporation of protein mobility and structural water heterogeneity in AutoDock, Proteins: Structure, Function, and Bioinformatics, vol.37, issue.1, pp.34-40, 2002.
DOI : 10.1002/(SICI)1097-0134(19991101)37:2<228::AID-PROT8>3.0.CO;2-8

G. Otting and K. Wuthrich, Heteronuclear filters in two-dimensional [ 1 H, 1990.

H. Spectroscopy, combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions, Q Rev Biophys, vol.23, pp.39-96

N. Ouyang, Y. G. Gao, H. Y. Hu, and Z. X. Xia, Crystal structures of E. coli CcmG and its mutants reveal key roles of the N-terminal ??-sheet and the fingerprint region, Proteins: Structure, Function, and Bioinformatics, vol.11, issue.4, pp.1021-1052, 2006.
DOI : 10.1110/ps.8.1.96

J. R. Pedrajas, A. Miranda-vizuete, N. Javanmardy, J. A. Gustafsson, and G. Spyrou, Contain One-conserved Cysteine Type Peroxiredoxin with Thioredoxin Peroxidase Activity, Journal of Biological Chemistry, vol.261, issue.21, pp.16296-301, 2000.
DOI : 10.1074/jbc.274.8.4722

URL : http://www.jbc.org/content/275/21/16296.full.pdf

G. Pugalenthi, K. Shameer, N. Srinivasan, and R. Sowdhamini, HARMONY: a server for the assessment of protein structures, Nucleic Acids Research, vol.34, issue.Web Server, pp.231-235, 2006.
DOI : 10.1093/nar/gkl314

J. Qin, G. M. Clore, W. M. Kennedy, J. R. Huth, and A. M. Gronenborn, Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF??B, Structure, vol.3, issue.3, pp.289-97, 1995.
DOI : 10.1016/S0969-2126(01)00159-9

J. Qin, G. M. Clore, W. P. Kennedy, J. Kuszewski, and A. M. Gronenborn, The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal, Structure, vol.4, issue.5, pp.613-633, 1996.
DOI : 10.1016/S0969-2126(96)00065-2

F. M. Ranaivoson, B. Kauffmann, F. Neiers, J. Wu, S. Boschi-muller et al., The X-ray Structure of the N-terminal Domain of PILB from Neisseria meningitidis Reveals a Thioredoxin-fold, Journal of Molecular Biology, vol.358, issue.2, pp.443-54, 2006.
DOI : 10.1016/j.jmb.2006.02.025

URL : https://hal.archives-ouvertes.fr/hal-00089656

J. Regeimbal, S. Gleiter, B. L. Trumpower, C. A. Yu, M. Diwakar et al., Disulfide bond formation involves a quinhydrone-type charge-transfer complex, Proceedings of the National Academy of Sciences, vol.273, issue.17, pp.13779-84, 2003.
DOI : 10.1074/jbc.273.17.10302

URL : http://www.pnas.org/content/100/24/13779.full.pdf

A. Rietsch, P. Bessette, G. Georgiou, and J. Beckwith, Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin., Journal of Bacteriology, vol.179, issue.21, pp.6602-6610, 1997.
DOI : 10.1128/jb.179.21.6602-6608.1997

A. Rozhkova and R. Glockshuber, Thermodynamic Aspects of DsbD-Mediated Electron Transport, Journal of Molecular Biology, vol.380, issue.5, pp.783-791, 2008.
DOI : 10.1016/j.jmb.2008.05.050

Y. Ryabov and D. Fushman, Structural Assembly of Multidomain Proteins and Protein Complexes Guided by the Overall Rotational Diffusion Tensor, Journal of the American Chemical Society, vol.129, issue.25, pp.7894-902, 2007.
DOI : 10.1021/ja071185d

R. Santucci, F. Sinibaldi, and L. Fiorucci, Protein Folding, Unfolding and Misfolding: Role Played by Intermediate States, Mini-Reviews in Medicinal Chemistry, vol.8, issue.1, pp.57-62, 2008.
DOI : 10.2174/138955708783331522

C. Schoneich, Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, 2005.
DOI : 10.1016/j.bbapap.2004.09.009

K. L. Seib, H. J. Tseng, A. G. Mcewan, M. A. Apicella, and M. P. Jennings, Distinctive Systems for Different Lifestyles, The Journal of Infectious Diseases, vol.190, issue.1, pp.136-183, 2004.
DOI : 10.1086/421299

K. L. Seib, H. J. Wu, S. P. Kidd, M. A. Apicella, M. P. Jennings et al., Defenses against Oxidative Stress in Neisseria gonorrhoeae: a System Tailored for a Challenging Environment, Microbiology and Molecular Biology Reviews, vol.70, issue.2, pp.344-61, 2006.
DOI : 10.1128/MMBR.00044-05

M. S. Seo, S. W. Kang, K. Kim, I. C. Baines, T. H. Lee et al., Identification of a New Type of Mammalian Peroxiredoxin That Forms an Intramolecular Disulfide as a Reaction Intermediate, Journal of Biological Chemistry, vol.333, issue.27, pp.20346-54, 2000.
DOI : 10.1042/bj3330291

C. S. Sevier and C. A. Kaiser, Formation and transfer of disulphide bonds in living cells, Nature Reviews Molecular Cell Biology, vol.239, issue.11, pp.836-883, 2002.
DOI : 10.1006/bbrc.1997.7426

F. Shao, M. W. Bader, U. Jakob, and J. C. Bardwell, DsbG, a Protein Disulfide Isomerase with Chaperone Activity, Journal of Biological Chemistry, vol.269, issue.18, pp.13349-52, 2000.
DOI : 10.1074/jbc.270.13.7288

S. B. Shuker, P. J. Hajduk, R. P. Meadows, and S. W. Fesik, Discovering High-Affinity Ligands for Proteins: SAR by NMR, Science, vol.274, issue.5292, pp.1531-1535, 1996.
DOI : 10.1126/science.274.5292.1531

K. T. Simons, R. Bonneau, I. Ruczinski, and D. Baker, Ab initio protein structure prediction of CASP III targets using ROSETTA, Proteins: Structure, Function, and Genetics, vol.277, issue.S3, pp.171-177, 1999.
DOI : 10.1002/(SICI)1097-0134(1999)37:3+<171::AID-PROT21>3.0.CO;2-Z

E. P. Skaar, D. M. Tobiason, J. Quick, R. C. Judd, H. Weissbach et al., The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species, Proceedings of the National Academy of Sciences, vol.40, issue.2, pp.10108-10121, 2002.
DOI : 10.1016/0092-8674(85)90143-6

C. A. Spronk, A. M. Bonvin, P. K. Radha, G. Melacini, R. Boelens et al., The solution structure of Lac repressor headpiece 62 complexed to a symmetrical lac operator, Structure, vol.7, issue.12, pp.1483-92, 1999.
DOI : 10.1016/S0969-2126(00)88339-2

T. M. Stevanin, J. W. Moir, and R. C. Read, Nitric Oxide Detoxification Systems Enhance Survival of Neisseria meningitidis in Human Macrophages and in Nasopharyngeal Mucosa, Infection and Immunity, vol.73, issue.6, pp.3322-3331, 2005.
DOI : 10.1128/IAI.73.6.3322-3329.2005

E. J. Stewart, F. Katzen, and J. Beckwith, Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli, The EMBO Journal, vol.18, issue.21, pp.5963-71, 1999.
DOI : 10.1093/emboj/18.21.5963

C. U. Stirnimann, M. G. Grutter, R. Glockshuber, and G. Capitani, nDsbD: a redox interaction hub in the Escherichia coli periplasm, Cellular and Molecular Life Sciences, vol.63, issue.14, pp.1642-1650, 2006.
DOI : 10.1007/s00018-006-6055-1

C. U. Stirnimann, A. Rozhkova, U. Grauschopf, R. A. Bockmann, R. Glockshuber et al., High-resolution Structures of Escherichia coli cDsbD in Different Redox States: A Combined Crystallographic, Biochemical and Computational Study, Journal of Molecular Biology, vol.358, issue.3, pp.829-874, 2006.
DOI : 10.1016/j.jmb.2006.02.030

C. U. Stirnimann, A. Rozhkova, U. Grauschopf, M. G. Grutter, R. Glockshuber et al., Structural Basis and Kinetics of DsbD-Dependent Cytochrome c Maturation, Structure, vol.13, issue.7, pp.985-93, 2005.
DOI : 10.1016/j.str.2005.04.014

X. X. Sun and C. C. Wang, DsbC, Journal of Biological Chemistry, vol.333, issue.30, pp.22743-22752, 2000.
DOI : 10.1093/emboj/17.4.927

M. K. Taha, P. C. Morand, Y. Pereira, E. Eugene, D. Giorgini et al., Pilus-mediated adhesion of Neisseria meningitidis: the essential role of cell contact-dependent transcriptional upregulation of the PilC1 protein, Molecular Microbiology, vol.273, issue.6, pp.1153-63, 1998.
DOI : 10.1126/science.273.5279.1234

J. T. Tan and J. C. Bardwell, Key Players Involved in Bacterial Disulfide-Bond Formation, ChemBioChem, vol.26, issue.11, pp.1479-87, 2004.
DOI : 10.1016/S1046-5928(02)00502-8

J. R. Tolman, H. M. Hashimi, L. E. Kay, and J. H. Prestegard, Structural and Dynamic Analysis of Residual Dipolar Coupling Data for Proteins, Journal of the American Chemical Society, vol.123, issue.7, pp.1416-1440, 2001.
DOI : 10.1021/ja002500y

A. Tovchigrechko and I. A. Vakser, GRAMM-X public web server for protein-protein docking, Nucleic Acids Research, vol.34, issue.Web Server, pp.310-314, 2006.
DOI : 10.1093/nar/gkl206

G. Vriend, WHAT IF: A molecular modeling and drug design program, Journal of Molecular Graphics, vol.8, issue.1, pp.52-58, 1990.
DOI : 10.1016/0263-7855(90)80070-V

N. Wakasugi, Y. Tagaya, H. Wakasugi, A. Mitsui, M. Maeda et al., Adult T-cell leukemia-derived factor/thioredoxin, produced by both human T-lymphotropic virus type I- and Epstein-Barr virus-transformed lymphocytes, acts as an autocrine growth factor and synergizes with interleukin 1 and interleukin 2., Proceedings of the National Academy of Sciences, vol.87, issue.21, pp.8282-8288, 1990.
DOI : 10.1073/pnas.87.21.8282

O. Walker, R. Varadan, and D. Fushman, Efficient and accurate determination of the overall rotational diffusion tensor of a molecule from 15N relaxation data using computer program ROTDIF, Journal of Magnetic Resonance, vol.168, issue.2, pp.336-381, 2004.
DOI : 10.1016/j.jmr.2004.03.019

C. Wang, M. Rance, and A. G. Palmer, Mapping Chemical Exchange in Proteins with MW > 50 kD, Journal of the American Chemical Society, vol.125, issue.30, pp.8968-8977, 2003.
DOI : 10.1021/ja035139z

A. Weichsel, J. R. Gasdaska, G. Powis, and W. R. Montfort, Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer, Structure, vol.4, issue.6, pp.735-51, 1996.
DOI : 10.1016/S0969-2126(96)00079-2

B. Whitehead, C. J. Craven, and J. P. Waltho, Double and Triple Resonance NMR Methods for Protein Assignment, Methods Mol Biol, vol.60, pp.29-52, 1997.
DOI : 10.1385/0-89603-309-0:29

M. Wiederstein and M. J. Sippl, ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins, Nucleic Acids Research, vol.35, issue.Web Server, pp.407-417, 2007.
DOI : 10.1093/nar/gkm290

D. S. Wishart, B. D. Sykes, and F. M. Richards, Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, Journal of Molecular Biology, vol.222, issue.2, pp.311-344, 1991.
DOI : 10.1016/0022-2836(91)90214-Q

D. S. Wishart and B. D. Sykes, [12] Chemical shifts as a tool for structure determination, Methods Enzymol, vol.239, pp.363-92, 1994.
DOI : 10.1016/S0076-6879(94)39014-2

D. S. Wishart and B. D. Sykes, The 13 C chemical-shift index: a simple method for the identification of protein secondary structure using 13 C chemical-shift data, J Biomol NMR, vol.4, pp.171-80, 1994.

H. J. Wu, K. L. Seib, J. L. Edwards, M. A. Apicella, A. G. Mcewan et al., Azurin of Pathogenic Neisseria spp. Is Involved in Defense against Hydrogen Peroxide and Survival within Cervical Epithelial Cells, Infection and Immunity, vol.73, issue.12, pp.8444-8452, 2005.
DOI : 10.1128/IAI.73.12.8444-8448.2005

J. Wu, F. Neiers, S. Boschi-muller, and G. Branlant, Is a Disulfide Reductase That Can Recycle Methionine Sulfoxide Reductases, Journal of Biological Chemistry, vol.254, issue.13, pp.12344-50, 2005.
DOI : 10.1128/JB.184.7.2005-2018.2002

URL : https://hal.archives-ouvertes.fr/hal-01690798

M. Wunderlich and R. Glockshuber, In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA), J Biol Chem, vol.268, pp.24547-50, 1993.

T. Xie, L. Yu, M. W. Bader, J. C. Bardwell, and C. A. Yu, Identification of the Ubiquinone-binding Domain in the Disulfide Catalyst Disulfide Bond Protein B, Journal of Biological Chemistry, vol.260, issue.3, pp.1649-52, 2002.
DOI : 10.1073/pnas.97.20.10884

Y. Xu, J. Wu, D. Gorenstein, and W. Braun, Automated 2D NOESY Assignment and Structure Calculation of Crambin(S22/I25) with the Self-Correcting Distance Geometry Based NOAH/DIAMOD Programs, Journal of Magnetic Resonance, vol.136, issue.1, pp.76-85, 1999.
DOI : 10.1006/jmre.1998.1616

A. Zapun, J. C. Bardwell, and T. E. Creighton, The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo, Biochemistry, vol.32, issue.19, pp.5083-92, 1993.
DOI : 10.1021/bi00070a016

C. Zwahlen, P. Legault, S. J. Vincent, J. Greenblatt, R. Konrat et al., RNA Complex, Journal of the American Chemical Society, vol.119, issue.29, pp.6711-6721, 1997.
DOI : 10.1021/ja970224q

J. Chung, T. Chen, and D. Missiakas, Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm, Molecular Microbiology, vol.34, issue.5, pp.1099-1109, 2000.
DOI : 10.1021/bi00015a019

E. H. Gordon, M. D. Page, A. C. Willis, F. , and S. J. , Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function, Molecular Microbiology, vol.289, issue.6, pp.1360-1374, 2000.
DOI : 10.1038/287396a0

P. W. Haebel, D. Goldstone, F. Katzen, J. Beckwith, and P. Metcalf, The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex, The EMBO Journal, vol.21, issue.18, pp.4774-4784, 2002.
DOI : 10.1093/emboj/cdf489

A. Rietsch, D. Belin, N. Martin, and J. Beckwith, An in vivo pathway for disulfide bond isomerization in Escherichia coli, Proceedings of the National Academy of Sciences, vol.90, issue.3, pp.13048-13053, 1996.
DOI : 10.1073/pnas.90.3.1038

A. Rietsch, P. Bessette, G. Georgiou, and J. Beckwith, Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin., Journal of Bacteriology, vol.179, issue.21, pp.6602-6608, 1997.
DOI : 10.1128/jb.179.21.6602-6608.1997

F. Katzen and J. Beckwith, Transmembrane Electron Transfer by the Membrane Protein DsbD Occurs via a Disulfide Bond Cascade, Cell, vol.103, issue.5, pp.769-779, 2000.
DOI : 10.1016/S0092-8674(00)00180-X

R. Krupp, C. Chan, and D. Missiakas, DsbD-catalyzed transport of electrons across the membrane of Escherichia coli, 2001.

J. F. Collet, J. Riemer, M. W. Bader, and J. C. Bardwell, Reconstitution of a Disulfide Isomerization System, Journal of Biological Chemistry, vol.14, issue.30, pp.26886-26892, 2002.
DOI : 10.1021/bi00070a016

R. A. Fabianek, H. Hennecke, and L. Thony-meyer, The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo, J. Bacteriol, vol.180, 1947.

R. A. Fabianek, T. Hofer, and L. Thony-meyer, Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation, Archives of Microbiology, vol.171, issue.2, pp.92-100, 1999.
DOI : 10.1007/s002030050683

E. Reid, J. Cole, and D. J. Eaves, The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly, Biochemical Journal, vol.355, issue.1, pp.51-58, 2001.
DOI : 10.1042/bj3550051

P. H. Bessette, J. J. Cotto, H. F. Gilbert, and G. Georgiou, Periplasmic Cysteine Oxidoreductase DsbG, Journal of Biological Chemistry, vol.172, issue.12, pp.7784-7792, 1999.
DOI : 10.1021/bi00407a034

A. Rozhkova, C. U. Stirnimann, P. Frei, U. Grauschopf, R. Brunisholz et al., Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD, The EMBO Journal, vol.34, issue.8, pp.1709-1719, 2004.
DOI : 10.1038/sj.emboj.7600178

C. U. Stirnimann, A. Rozhkova, U. Grauschopf, M. G. Gruetter, R. Glockshuber et al., Structural Basis and Kinetics of DsbD-Dependent Cytochrome c Maturation, Structure, vol.13, issue.7, pp.985-993, 2005.
DOI : 10.1016/j.str.2005.04.014

N. Brot, J. F. Collet, L. C. Johnson, T. J. Jonsson, H. Weissbach et al., PilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases, Journal of Biological Chemistry, vol.348, issue.43, pp.32668-32675, 2006.
DOI : 10.1002/elps.1150181505

R. Keller, Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment, 2004.

D. S. Wishart, C. G. Bigam, J. Yao, F. Abildgaard, H. J. Dyson et al., ) 1 H, 13 C and 15 N chemical shift referencing in biomolecular NMR, J. Biomol. NMR, vol.6, pp.135-140, 1995.

Y. Bai, J. S. Milne, L. Mayne, and S. W. Englander, Primary structure effects on peptide group hydrogen exchange, Proteins: Structure, Function, and Genetics, vol.6, issue.1, pp.75-86, 1993.
DOI : 10.1016/0022-2364(85)90018-6

F. Cordier and S. Grzesiek, Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR, J. Mol. Biol, vol.317, pp.39-52, 2002.
URL : https://hal.archives-ouvertes.fr/pasteur-00367132

F. Cordier, M. Barfield, and S. Grzesiek, Scalar Couplings, Journal of the American Chemical Society, vol.125, issue.51, pp.15750-15751, 2003.
DOI : 10.1021/ja038616m

URL : https://hal.archives-ouvertes.fr/pasteur-00367130

T. Herrmann, P. Güntert, and K. Wüthrich, Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS, Journal of Biomolecular NMR, vol.24, issue.3, pp.171-189, 2002.
DOI : 10.1023/A:1021614115432

T. Herrmann, P. Güntert, and K. Wüthrich, Protein NMR Structure Determination with Automated NOE Assignment Using the New Software CANDID and the Torsion Angle Dynamics Algorithm DYANA, Journal of Molecular Biology, vol.319, issue.1, pp.209-227, 2002.
DOI : 10.1016/S0022-2836(02)00241-3

G. Cornilescu, F. Delaglio, and A. Bax, Protein backbone angle restraints from searching a database for chemical shift and sequence homology, Journal of Biomolecular NMR, vol.13, issue.3, pp.289-302, 1999.
DOI : 10.1023/A:1008392405740

P. Guntert, Automated NMR Structure Calculation With CYANA, Methods Mol. Biol, vol.278, pp.353-378, 2004.
DOI : 10.1385/1-59259-809-9:353

R. Koradi, M. Billeter, and K. Wüthrich, MOLMOL: A program for display and analysis of macromolecular structures, Journal of Molecular Graphics, vol.14, issue.1, pp.51-55, 1996.
DOI : 10.1016/0263-7855(96)00009-4

N. A. Farrow, R. Muhandiram, A. U. Singer, S. M. Pascal, C. M. Kay et al., Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR Relaxation, Biochemistry, vol.33, issue.19, pp.5984-6003, 1994.
DOI : 10.1021/bi00185a040

B. A. Johnson and R. A. Blevins, NMR View: A computer program for the visualization and analysis of NMR data, Journal of Biomolecular NMR, vol.88, issue.5, pp.603-614, 1994.
DOI : 10.1007/BF00404272

N. A. Farrow, O. Zhang, A. Szabo, D. A. Torchia, K. et al., Spectral density function mapping using 15 N relaxation data exclusively, J. Biomol. NMR, vol.6, pp.153-162, 1995.
DOI : 10.1007/bf00211779

R. Ishima, K. Yamasaki, M. Saito, and K. Nagayama, Spectral densities of nitrogen nuclei in Escherichia coli ribonuclease HI obtained by 15 N NMR relaxation and molecular dynamics, 1995.

R. Ishima and K. Nagayama, Protein Backbone Dynamics Revealed by Quasi Spectral Density Function Analysis of Amide N-15 Nuclei, Biochemistry, vol.34, issue.10, pp.3162-3171, 1995.
DOI : 10.1021/bi00010a005

Y. Hiyama, C. Niu, J. V. Silverton, A. Bavoso, and D. A. Torchia, Determination of 15 N chemical shift tensor via 15 N- 2 H dipolar coupling in Boc-glycylglycyl[ 15 N glycine, 1988.

J. W. Peng and G. Wagner, Frequency Spectrum of NH Bonds in Eglin c from Spectral Density Mapping at Multiple Fields, Biochemistry, vol.34, issue.51, pp.16733-16752, 1995.
DOI : 10.1021/bi00051a023

P. Dosset, J. Hus, M. Blackledge, M. , and D. , Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data, Journal of Biomolecular NMR, vol.16, issue.1, pp.23-28, 2000.
DOI : 10.1023/A:1008305808620

G. Lipari and A. Szabo, Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity, Journal of the American Chemical Society, vol.104, issue.17, pp.4546-4559, 1982.
DOI : 10.1021/ja00381a009

G. Lipari and A. Szabo, Model-free approach to the interpretation on nuclear magnetic resonance relaxation in macromolecules . 2. Analysis of experimental results, J. Am. Chem. Soc, vol.104, pp.4560-4570, 1982.

M. Quinternet, L. Selme, P. Tsan, C. Beaufils, C. Jacob et al., 1H, 13C, and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis, Biomolecular NMR Assignments, vol.4, issue.1, pp.85-87, 2008.
DOI : 10.1007/s12104-008-9091-y

URL : https://hal.archives-ouvertes.fr/hal-00433190

R. A. Laskowski, J. A. Rullmann, M. W. Macarthur, R. Kaptein, T. et al., AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR, Journal of Biomolecular NMR, vol.8, issue.4, pp.477-486, 1996.
DOI : 10.1007/BF00228148

G. Vriend and C. Sander, Quality control of protein models: directional atomic contact analysis, Journal of Applied Crystallography, vol.26, issue.1, pp.47-60, 1993.
DOI : 10.1107/S0021889892008240

L. Holm and C. Sander, Protein Structure Comparison by Alignment of Distance Matrices, Journal of Molecular Biology, vol.233, issue.1, pp.123-138, 1993.
DOI : 10.1006/jmbi.1993.1489

J. F. Gibrat, T. Madej, and S. H. Bryant, Surprising similarities in structure comparison, Current Opinion in Structural Biology, vol.6, issue.3, pp.377-385, 1996.
DOI : 10.1016/S0959-440X(96)80058-3

L. Guignard, A. Padilla, J. Mispelter, Y. S. Yang, M. H. Stern et al., Backbone dynamics and solution structure refinement of the 15 N-labeled human oncogenic protein p13 MTCP1 : comparison with X-ray data, Journal of Biomolecular NMR, vol.17, issue.3, pp.215-230, 2000.
DOI : 10.1023/A:1008386110930

K. L. Constantine, M. S. Friedrichs, V. Goldfarb, P. D. Jeffrey, S. Sheriff et al., Characterization of the backbone dynamics of an anti-digoxin antibody VL domain by inverse detected1H-15N NMR: Comparisons with X-ray data for the Fab, Proteins: Structure, Function, and Genetics, vol.82, issue.3, pp.290-311, 1993.
DOI : 10.1016/0022-2364(89)90391-0

C. U. Stirnimann, M. G. Grütter, R. Glockshuber, C. , and G. , nDsbD: a redox interaction hub in the Escherichia coli periplasm, Cellular and Molecular Life Sciences, vol.63, issue.14, pp.1642-1648, 2006.
DOI : 10.1007/s00018-006-6055-1

P. Gouet, E. Courcelle, D. I. Stuart, and F. Metoz, ESPript: analysis of multiple sequence alignments in PostScript, Bioinformatics, vol.15, issue.4, pp.305-308, 1999.
DOI : 10.1093/bioinformatics/15.4.305

URL : https://hal.archives-ouvertes.fr/hal-00314288

R. Bartels, C. Xia, T. Billeter, M. Güntert, P. Wüthrich et al., The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, Journal of Biomolecular NMR, vol.285, issue.1, pp.1-10, 1995.
DOI : 10.1016/0022-2364(88)90203-X

C. Beaufils, F. Neiers, N. Coudevylle, S. Boschi-muller, M. Averlant-petit et al., 1 H, 13 C and 15 N resonance assignment of the N-terminal domain of PilB from Neisseria meningitides, J Biomol NMR, vol.36, issue.6, 2006.
URL : https://hal.archives-ouvertes.fr/hal-00199133

S. Boschi-muller, A. Olry, M. Antoine, and G. Branlant, The enzymology and biochemistry of methionine sulfoxide reductases, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, pp.231-238, 2005.
DOI : 10.1016/j.bbapap.2004.09.016

URL : https://hal.archives-ouvertes.fr/hal-01690795

G. Cornilescu, F. Delaglio, A. Bax, S. Boschi-muller, S. Azza et al., Protein backbone angle REFERENCES 1 A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli, 1999.

S. Boschi-muller, A. Olry, M. Antoine, and G. Branlant, The enzymology and biochemistry of methionine sulfoxide reductases, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1703, issue.2, pp.231-238, 2005.
DOI : 10.1016/j.bbapap.2004.09.016

URL : https://hal.archives-ouvertes.fr/hal-01690795

E. P. Skaar, D. M. Tobiason, J. Quick, R. C. Judd, H. Weissbach et al., The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species, Proc. Natl, 2002.
DOI : 10.1016/0092-8674(85)90143-6

J. Wu, F. Neiers, S. Boschi-muller, and G. Branlant, The N-terminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductases, 2005.
URL : https://hal.archives-ouvertes.fr/hal-01690798

F. M. Ranaivoson, B. Kauffmann, F. Neiers, J. Wu, S. Boschi-muller et al., The X-ray Structure of the N-terminal Domain of PILB from Neisseria meningitidis Reveals a Thioredoxin-fold, Journal of Molecular Biology, vol.358, issue.2, pp.443-454, 2006.
DOI : 10.1016/j.jmb.2006.02.025

URL : https://hal.archives-ouvertes.fr/hal-00089656

N. Brot, J. F. Collet, L. C. Johnson, T. J. Jönsson, H. Weissbach et al., PilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases, Journal of Biological Chemistry, vol.348, issue.43, pp.32668-32675, 2006.
DOI : 10.1002/elps.1150181505

R. A. Fabianek, H. Hennecke, and L. Thöny-meyer, The active-site cysteines of the periplasmic thioredoxin-like protein in CcmG of Escherichia coli are important but not essential for cytochrome c maturation vivo, J. Bacteriol, vol.180, 1947.

R. A. Fabianek, M. Huber-wunderlich, R. Glockshuber, P. Künzler, H. Hennecke et al., -Type Cytochromes, Journal of Biological Chemistry, vol.178, issue.7, pp.4467-4473, 1997.
DOI : 10.1128/jb.178.21.6166-6172.1996

H. Loferer, M. Bott, and H. Hennecke, Bradyrhizobium japonicum TlpA, a novel membrane-anchored thioredoxin-like protein involved in the biogenesis of cytochrome aa3 and development of symbiosis, EMBO J, vol.12, pp.3373-3383, 1993.

L. S. Erlendsson, R. M. Acheson, L. Hederstedt, L. Brun, and N. E. , Synthesis, Journal of Biological Chemistry, vol.1504, issue.20, pp.17852-17858, 2003.
DOI : 10.1016/S0005-2728(00)00265-6

N. Ouyang, Y. G. Gao, H. Y. Hu, and Z. X. Xia, Crystal structures of E. coli CcmG and its mutants reveal key roles of the N-terminal ??-sheet and the fingerprint region, Proteins: Structure, Function, and Bioinformatics, vol.11, issue.4, pp.1021-1031, 2006.
DOI : 10.1110/ps.8.1.96

M. A. Edeling, L. W. Guddat, R. A. Fabianek, L. Thöny-meyer, M. et al., Structure of CcmG/DsbE at 1.14 ?? Resolution, Structure, vol.10, issue.7, pp.973-979, 2002.
DOI : 10.1016/S0969-2126(02)00794-3

G. Capitani, R. Rossmann, D. F. Sargent, M. G. Grütter, T. J. Richmond et al., Structure of the soluble domain of a membrane-anchored thioredoxin-like protein from Bradyrhizobium japonicum reveals unusual properties11Edited by R. Huber, Journal of Molecular Biology, vol.311, issue.5, pp.1037-1048, 2001.
DOI : 10.1006/jmbi.2001.4913

A. Crow, R. M. Acheson, N. E. Le-brun, and A. Oubrie, Biosynthesis Protein ResA, Journal of Biological Chemistry, vol.3, issue.22, pp.23654-23660, 2004.
DOI : 10.1002/prot.340110407

X. Zhang, Y. Hu, X. Guo, E. Lescop, Y. Li et al., YkuV Is a Thiol:Disulfide Oxidoreductase Revealed by Its Redox Structures and Activity, Journal of Biological Chemistry, vol.4, issue.12, pp.8296-8304, 2006.
DOI : 10.1006/jmbi.1999.3034

C. Bartels, T. Xia, M. Billeter, P. Güntert, and K. Wüthrich, The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, Journal of Biomolecular NMR, vol.285, issue.1, pp.1-10, 1995.
DOI : 10.1016/0022-2364(88)90203-X

R. Keller, Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment, 2004.

D. S. Wishart, C. G. Bigam, J. Yao, F. Abildgaard, H. J. Dyson et al., ) 1 H, 13 C and 15 N chemical shift referencing in biomolecular NMR, J. Biomol. NMR, vol.6, pp.135-140, 1995.

Y. Bai, J. S. Milne, L. Mayne, and S. W. Englander, Primary structure effects on peptide group hydrogen exchange, Proteins: Structure, Function, and Genetics, vol.6, issue.1, pp.75-86, 1993.
DOI : 10.1016/0022-2364(85)90018-6

F. Cordier and S. Grzesiek, Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR, J. Mol. Biol, vol.317, pp.39-52, 2002.
URL : https://hal.archives-ouvertes.fr/pasteur-00367132

G. Cornilescu, F. Delaglio, and A. Bax, Protein backbone angle restraints from searching a database for chemical shift and sequence homology, Journal of Biomolecular NMR, vol.13, issue.3, pp.289-302, 1999.
DOI : 10.1023/A:1008392405740

I. Z. Siemion, T. Wieland, and K. H. Pook, Influence of the Distance of the Proline Carbonyl from the ? and ? Carbon on the13C Chemical Shifts, Angewandte Chemie International Edition in English, vol.343, issue.10, pp.702-703, 1975.
DOI : 10.1016/0304-4165(74)90286-4

P. Guntert, C. Mumenthaler, and K. Wüthrich, Torsion angle dynamics for NMR structure calculation with the new program Dyana, Journal of Molecular Biology, vol.273, issue.1, pp.283-298, 1997.
DOI : 10.1006/jmbi.1997.1284

P. Guntert, Automated NMR Structure Calculation With CYANA, Methods Mol. Biol, vol.278, pp.353-378, 2004.
DOI : 10.1385/1-59259-809-9:353

R. Koradi, M. Billeter, and K. Wüthrich, MOLMOL: A program for display and analysis of macromolecular structures, Journal of Molecular Graphics, vol.14, issue.1, pp.51-55, 1996.
DOI : 10.1016/0263-7855(96)00009-4

N. A. Farrow, R. Muhandiram, A. U. Singer, S. M. Pascal, C. M. Kay et al., Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR Relaxation, Biochemistry, vol.33, issue.19, pp.5984-6003, 1994.
DOI : 10.1021/bi00185a040

B. A. Johnson and R. A. Blevins, NMR View: A computer program for the visualization and analysis of NMR data, Journal of Biomolecular NMR, vol.88, issue.5, pp.603-614, 1994.
DOI : 10.1007/BF00404272

N. A. Farrow, O. Zhang, A. Szabo, D. A. Torchia, K. et al., Spectral density function mapping using 15 N relaxation data exclusively, J. Biomol. NMR, vol.6, pp.153-162, 1995.

R. Ishima, K. Yamasaki, M. Saito, and K. Nagayama, Spectral densities of nitrogen nuclei in Escherichia coli ribonuclease HI obtained by 15 N NMR relaxation and molecular dynamics, 1995.

R. Ishima and K. Nagayama, Protein Backbone Dynamics Revealed by Quasi Spectral Density Function Analysis of Amide N-15 Nuclei, Biochemistry, vol.34, issue.10, pp.3162-3171, 1995.
DOI : 10.1021/bi00010a005

Y. Hiyama, C. Niu, J. V. Silverton, A. Bavoso, and D. A. Torchia, Determination of 15 N chemical shift tensor via 15 N- 2 H dipolar coupling in Boc-glycylglycyl[ 15 N glycine, 1988.

J. W. Peng and G. Wagner, Frequency Spectrum of NH Bonds in Eglin c from Spectral Density Mapping at Multiple Fields, Biochemistry, vol.34, issue.51, pp.16733-16752, 1995.
DOI : 10.1021/bi00051a023

P. Dosset, J. Hus, M. Blackledge, M. , and D. , Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data, Journal of Biomolecular NMR, vol.16, issue.1, pp.23-28, 2000.
DOI : 10.1023/A:1008305808620

G. Lipari and A. Szabo, Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity, Journal of the American Chemical Society, vol.104, issue.17, pp.4546-4559, 1982.
DOI : 10.1021/ja00381a009

G. Lipari and A. Szabo, Model-free approach to the interpretation on nuclear magnetic resonance relaxation in macromolecules . 2. Analysis of experimental results, J. Am. Chem. Soc, vol.104, pp.4560-4570, 1982.

C. Beaufils, F. Neiers, N. Coudevylle, S. Boschi-muller, M. C. Averlant-petit et al., ) 1 H, 13 C and 15 N resonance assignment of the N-terminal domain of PilB from Neisseria meningitidis, J. Biomol. NMR, vol.36, issue.6, 2006.

M. Quinternet, C. Beaufils, F. Neiers, P. Tsan, S. Boschi-muller et al., 1H, 13C and 15N resonance assignment of the oxidized form (Cys67???Cys70) of the N-terminal domain of PilB from Neisseria meningitidis, Biomolecular NMR Assignments, vol.280, issue.1, pp.143-145, 2007.
DOI : 10.1016/j.bbapap.2004.09.016

URL : https://hal.archives-ouvertes.fr/hal-00433195

D. Auguin, P. Barthe, M. T. Augé-sénégas, M. H. Stern, M. Noguchi et al., Solution Structure and Backbone Dynamics of the Pleckstrin Homology Domain of the Human Protein Kinase??B (PKB/Akt). Interaction with Inositol Phosphates, Journal of Biomolecular NMR, vol.28, issue.2, pp.137-155, 2004.
DOI : 10.1023/B:JNMR.0000013836.62154.c2

L. Holm and C. Sander, Protein Structure Comparison by Alignment of Distance Matrices, Journal of Molecular Biology, vol.233, issue.1, pp.123-138, 1993.
DOI : 10.1006/jmbi.1993.1489

J. F. Gibrat, T. Madej, and S. H. Bryant, Surprising similarities in structure comparison, Current Opinion in Structural Biology, vol.6, issue.3, pp.377-385, 1996.
DOI : 10.1016/S0959-440X(96)80058-3

H. M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T. N. Bhat et al., The Protein Data Bank, Nucleic Acids Research, vol.28, issue.1, pp.235-242, 2000.
DOI : 10.1093/nar/28.1.235

J. Lancelin, L. Guilhaudis, I. Krimm, M. J. Blackledge, D. Marion et al., NMR structures of thioredoxinm from the green algaChlamydomonas reinhardtii, Proteins: Structure, Function, and Genetics, vol.36, issue.3, pp.334-349, 2000.
DOI : 10.1110/ps.8.2.426

M. J. Stone, K. Chandrasekhar, A. Holmgren, P. E. Wright, D. et al., Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using nitrogen-15 NMR relaxation measurements, Biochemistry, vol.32, issue.2, pp.426-435, 1993.
DOI : 10.1021/bi00053a007

C. L. Colbert, Q. Wu, P. J. Erbel, K. H. Gardner, and J. Deisenhofer, Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation, Proceedings of the National Academy of Sciences, vol.4, issue.2, pp.4110-4415, 2006.
DOI : 10.1007/BF00175245

M. A. Hass, M. H. Thuesen, H. E. Christensen, and J. J. Led, N NMR Relaxation and Chemical Shift:?? Conformational Exchange in Plastocyanin Induced by Histidine Protonations, Journal of the American Chemical Society, vol.126, issue.3, pp.753-765, 2004.
DOI : 10.1021/ja030366m

C. U. Stirnimann, M. G. Grütter, R. Glockshuber, C. , and G. , nDsbD: a redox interaction hub in the Escherichia coli periplasm, Cellular and Molecular Life Sciences, vol.63, issue.14, pp.1642-1648, 2006.
DOI : 10.1007/s00018-006-6055-1

P. Gouet, E. Courcelle, D. I. Stuart, and F. Metoz, ESPript: analysis of multiple sequence alignments in PostScript, Bioinformatics, vol.15, issue.4, pp.305-308, 1999.
DOI : 10.1093/bioinformatics/15.4.305

URL : https://hal.archives-ouvertes.fr/hal-00314288

R. Koradi, M. Billeter, and K. Wüthrich, MOLMOL: A program for display and analysis of macromolecular structures, Journal of Molecular Graphics, vol.14, issue.1, pp.51-55, 1996.
DOI : 10.1016/0263-7855(96)00009-4

G. Lipari and A. Szabo, Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity, Journal of the American Chemical Society, vol.104, issue.17, pp.4546-4559, 1982.
DOI : 10.1021/ja00381a009

G. Lipari and A. Szabo, Model-free approach to the interpretation on nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results, J. Am. Chem, 1982.

A. Porat, S. H. Cho, and J. Beckwith, The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases, Research in Microbiology, vol.155, issue.8, pp.617-622, 2004.
DOI : 10.1016/j.resmic.2004.05.005

M. Quinternet, C. Beaufils, F. Neiers, P. Tsan, S. Boschi-muller et al., ) 1 H, 13 C and 15 N backbone resonance assignment of the oxidized form (Cys 67 - Cys 70, 2007.

M. Quinternet, P. Tsan, L. Selme, C. Beaufils, C. Jacob et al., Solution structure and backbone dynamics of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis, Biochemistry, vol.doi, p.10, 1021.

M. Quinternet, L. Selme, P. Tsan, C. Beaufils, C. Jacob et al., 1H, 13C, and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis, Biomolecular NMR Assignments, vol.4, issue.1, pp.85-87, 2008.
DOI : 10.1007/s12104-008-9091-y

URL : https://hal.archives-ouvertes.fr/hal-00433190

F. M. Ranaivoson, B. Kauffmann, F. Neiers, J. Wu, S. Boschi-muller et al., The X-ray Structure of the N-terminal Domain of PILB from Neisseria meningitidis Reveals a Thioredoxin-fold, Journal of Molecular Biology, vol.358, issue.2, pp.443-454, 2006.
DOI : 10.1016/j.jmb.2006.02.025

URL : https://hal.archives-ouvertes.fr/hal-00089656

A. Rozhkova, C. U. Stirnimann, P. Frei, U. Grauschopf, R. Brunisholz et al., Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD, The EMBO Journal, vol.34, issue.8, pp.1709-1719, 2004.
DOI : 10.1038/sj.emboj.7600178

E. J. Stewart, F. Katzen, and J. Beckwith, Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli, The EMBO Journal, vol.18, issue.21, 1999.
DOI : 10.1093/emboj/18.21.5963

C. U. Stirnimann, M. G. Grütter, R. Glockshuber, C. , and G. , nDsbD: a redox interaction hub in the Escherichia coli periplasm, Cellular and Molecular Life Sciences, vol.63, issue.14, pp.1642-1648, 2006.
DOI : 10.1007/s00018-006-6055-1

C. U. Stirnimann, A. Rozhkova, U. Grauschopf, M. G. Gruetter, R. Glockshuber et al., Structural Basis and Kinetics of DsbD-Dependent Cytochrome c Maturation, Structure, vol.13, issue.7, pp.985-993, 2005.
DOI : 10.1016/j.str.2005.04.014

S. C. Sue, C. Cervantes, E. A. Komives, D. , and H. J. , Transfer of Flexibility between Ankyrin Repeats in I??B?? upon Formation of the NF-??B Complex, Journal of Molecular Biology, vol.380, issue.5, pp.917-931, 2008.
DOI : 10.1016/j.jmb.2008.05.048

J. Wu, F. Neiers, S. Boschi-muller, and G. Branlant, The Nterminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductases, J. Biol, 2005.
URL : https://hal.archives-ouvertes.fr/hal-01690798

C. Zwahlen, P. Legault, S. Vincent, J. Greenblatt, R. Konrat et al., RNA Complex, Journal of the American Chemical Society, vol.119, issue.29, pp.6711-6721, 1997.
DOI : 10.1021/ja970224q

S. Data and S. , Reduced spectral density function at? N ) and J eff (0) for (A) nDsbD cx (?) compared to those of nDsbD free (?) (B) and of NterPilB cx (?) compared to those of NterPilB free in its oxidized form (?)

S. Data and S. , Superimposition of the X-ray Structure of nDsbD-SS-DsbE with the NMR Modeled Structure of nDsbD-SS-NterPilB

. Nterpilb, a grey ribbon for the NterPilB cx subunit of nDsbD-SS-NterPilB, a pink ribbon for the nDsbD partner of nDsbD-SS-DsbE and an orange ribbon for the DsbE partner of DsbD-SS-DsbE

S. Data and S. , Superimposition of N. meningitidis nDsbD free and nDsbD cx

S. Data and S. , NMR Spectroscopy for Assignment and 15 N Relaxation of the Mixed Disulfide Complex Between nDsbD and NterPilB from Neisseria Meningitidis

M. C. Averlant-petit, G. Branlant, and M. T. Cung, 1 H, 13 C and 15 N resonance assignment of the N-terminal domain of PilB from Neisseria meningitidis, J. Biomol. NMR, vol.36, issue.6, 2006.
URL : https://hal.archives-ouvertes.fr/hal-00433196

P. Dosset, J. C. Hus, M. Blackledge, M. , and D. , Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data, Journal of Biomolecular NMR, vol.16, issue.1, pp.23-28, 2000.
DOI : 10.1023/A:1008305808620

N. A. Farrow, R. Muhandiram, A. U. Singer, S. M. Pascal, C. M. Kay et al., Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR Relaxation, Biochemistry, vol.33, issue.19, pp.5984-6003, 1994.
DOI : 10.1021/bi00185a040

R. Ishima, K. Yamasaki, M. Saito, and K. Nagayama, Spectral densities of nitrogen nuclei in Escherichia coli ribonuclease HI obtained by 15 N NMR relaxation and molecular dynamics, J. Biomol. NMR, vol.2, pp.217-220, 1995.

R. Ishima and K. Nagayama, Protein Backbone Dynamics Revealed by Quasi Spectral Density Function Analysis of Amide N-15 Nuclei, Biochemistry, vol.34, issue.10, 1995.
DOI : 10.1021/bi00010a005

B. A. Johnson and R. A. Blevins, NMRView: A computer program for the visualization and analysis of NMR data, J. Biomol, 1994.

R. Keller, Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment, 2004.

G. Lipari and A. Szabo, Model-free approach to the interpretation on nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity, J. Am. Chem, 1982.

G. Lipari and A. Szabo, Model-free approach to the interpretation on nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results, J. Am. Chem, 1982.

J. W. Peng and G. Wagner, Frequency Spectrum of NH Bonds in Eglin c from Spectral Density Mapping at Multiple Fields, Biochemistry, vol.34, issue.51, pp.16733-16752, 1995.
DOI : 10.1021/bi00051a023

M. Quinternet, C. Beaufils, F. Neiers, P. Tsan, S. Boschi-muller et al., 1H, 13C and 15N resonance assignment of the oxidized form (Cys67???Cys70) of the N-terminal domain of PilB from Neisseria meningitidis, Biomolecular NMR Assignments, vol.280, issue.1, pp.143-145, 2007.
DOI : 10.1016/j.bbapap.2004.09.016

URL : https://hal.archives-ouvertes.fr/hal-00433195

S. Muller, M. C. Averlant-petit, G. Branlant, and M. T. Cung, 1 H, 13 C and 15 N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis, 2008.
URL : https://hal.archives-ouvertes.fr/hal-00433190

D. S. Wishart, C. G. Bigam, J. Yao, F. Abildgaard, H. J. Dyson et al., ) 1 H, 13 C and 15 N chemical shift referencing in biomolecular NMR, J. Biomol. NMR, vol.6, pp.135-140, 1995.

R. Bartels, C. Xia, T. Billeter, M. Güntert, P. Wüthrich et al., The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, Journal of Biomolecular NMR, vol.285, issue.1, pp.1-10, 1995.
DOI : 10.1016/0022-2364(88)90203-X

M. A. Edeling, L. W. Guddat, R. A. Fabianek, L. Thony-meyer, and J. L. Martin, Structure of CcmG/DsbE at 1.14 ?? Resolution, Structure, vol.10, issue.7, pp.973-982, 2002.
DOI : 10.1016/S0969-2126(02)00794-3

J. Wu, F. Neiers, S. Boschi-muller, and G. Branlant, Is a Disulfide Reductase That Can Recycle Methionine Sulfoxide Reductases, Journal of Biological Chemistry, vol.254, issue.13, pp.12344-12350, 2005.
DOI : 10.1128/JB.184.7.2005-2018.2002

URL : https://hal.archives-ouvertes.fr/hal-01690798