F. Raushel, Bacterial detoxification of organophosphate nerve agents, Current Opinion in Microbiology, vol.5, issue.3, pp.288-295, 2002.
DOI : 10.1016/S1369-5274(02)00314-4

B. Singh, Organophosphorus-degrading bacteria: ecology and industrial applications, Nature Reviews Microbiology, vol.150, issue.2, pp.156-164, 2009.
DOI : 10.1099/mic.0.26977-0

S. Caldwell, J. Newcomb, K. Schlecht, and F. Raushel, Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta, Biochemistry, vol.30, issue.30, pp.7438-7444, 1991.
DOI : 10.1021/bi00244a010

D. Vecchio, P. Elias, M. Merone, L. Graziano, G. Dupuy et al., Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus, Extremophiles, vol.4, issue.3, pp.461-470, 2009.
DOI : 10.1016/j.bbapap.2005.06.008

M. Elias, J. Dupuy, L. Merone, L. Mandrich, E. Porzio et al., Structural Basis for Natural Lactonase and Promiscuous Phosphotriesterase Activities, Journal of Molecular Biology, vol.379, issue.5, pp.1017-1028, 2008.
DOI : 10.1016/j.jmb.2008.04.022

L. Merone, L. Mandrich, M. Rossi, and G. Manco, A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties, Extremophiles, vol.185, issue.4, pp.297-305, 2005.
DOI : 10.1042/bj3320203

M. Elias and D. Tawfik, Divergence and Convergence in Enzyme Evolution: Parallel Evolution of Paraoxonases from Quorum-quenching Lactonases, Journal of Biological Chemistry, vol.267, issue.1, pp.11-20, 2012.
DOI : 10.1074/jbc.R111.240945

M. Ben-david, M. Elias, J. Filippi, E. Dunach, I. Silman et al., Catalytic Versatility and Backups in Enzyme Active Sites: The Case of Serum Paraoxonase 1, Journal of Molecular Biology, vol.418, issue.3-4, pp.181-196, 2012.
DOI : 10.1016/j.jmb.2012.02.042

E. Scharff, J. Koepke, G. Fritzsch, C. Lucke, and H. Ruterjans, Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris, Structure, vol.9, issue.6, pp.493-502, 2001.
DOI : 10.1016/S0969-2126(01)00610-4

J. Koepke, E. Scharff, C. Lucke, H. Ruterjans, and G. Fritzsch, Atomic resolution crystal structure of squid ganglion DFPase, Acta Crystallographica Section D Biological Crystallography, vol.58, issue.10, pp.1757-1759, 2002.
DOI : 10.1107/S0907444902012714

M. Blum, F. Lohr, A. Richardt, H. Ruterjans, and J. Chen, Binding of a Designed Substrate Analogue to Diisopropyl Fluorophosphatase:?? Implications for the Phosphotriesterase Mechanism, Journal of the American Chemical Society, vol.128, issue.39, pp.12750-12757, 2006.
DOI : 10.1021/ja061887n

M. Ben-david, G. Wieczorek, M. Elias, I. Silman, J. Sussman et al., Catalytic Metal Ion Rearrangements Underline Promiscuity and Evolvability of a Metalloenzyme, Journal of Molecular Biology, vol.425, issue.6, pp.1028-1038, 2013.
DOI : 10.1016/j.jmb.2013.01.009

J. Koepke, E. Scharff, C. Lucke, H. Ruterjans, and G. Fritzsch, Statistical analysis of crystallographic data obtained from squid ganglion DFPase at 0.85????? resolution, Acta Crystallographica Section D Biological Crystallography, vol.59, issue.10, pp.1744-1754, 2003.
DOI : 10.1107/S0907444903016135

E. Howard, R. Sanishvili, R. Cachau, A. Mitschler, B. Chevrier et al., Ultrahigh resolution drug design I: Details of interactions in human aldose reductase-inhibitor complex at 0.66 ??, Proteins: Structure, Function, and Bioinformatics, vol.40, issue.Suppl, pp.792-804, 2004.
DOI : 10.2172/369685

D. Liebschner, M. Elias, S. Moniot, B. Fournier, K. Scott et al., Elucidation of the Phosphate Binding Mode of DING Proteins Revealed by Subangstrom X-ray Crystallography, Journal of the American Chemical Society, vol.131, issue.22, pp.7879-7886, 2009.
DOI : 10.1021/ja901900y

M. Blum, M. Mustyakimov, H. Rüterjans, K. Kehe, B. Schoenborn et al., Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement, Proceedings of the National Academy of Sciences, vol.55, issue.Pt 10, pp.713-718, 2009.
DOI : 10.1107/S090744499900935X

J. Fraser, H. Van-den-bedem, A. Samelson, P. Lang, J. Holton et al., Accessing protein conformational ensembles using room-temperature X-ray crystallography, Proceedings of the National Academy of Sciences, vol.40, issue.3, pp.16247-16252, 2011.
DOI : 10.1002/1097-0134(20000815)40:3<389::AID-PROT50>3.0.CO;2-2

URL : http://www.pnas.org/content/108/39/16247.full.pdf

M. Elias, A. Wellner, K. Goldin-azulay, E. Chabriere, J. Vorholt et al., The molecular basis of phosphate discrimination in arsenate-rich environments, Nature, vol.314, issue.7422, pp.134-137, 2012.
DOI : 10.1038/314257a0

J. Vrettos and G. Brudvig, Water oxidation chemistry of photosystem II, Philosophical Transactions of the Royal Society B: Biological Sciences, vol.357, issue.1426, pp.1395-1404, 2002.
DOI : 10.1098/rstb.2002.1136

M. Blum, M. Mustyakimov, H. Ruterjans, K. Kehe, B. Schoenborn et al., Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement, Proceedings of the National Academy of Sciences, vol.55, issue.Pt 10, pp.713-718, 2009.
DOI : 10.1107/S090744499900935X

E. Ghanem and F. Raushel, Detoxification of organophosphate nerve agents by bacterial phosphotriesterase, Toxicology and Applied Pharmacology, vol.207, issue.2, pp.459-470, 2005.
DOI : 10.1016/j.taap.2005.02.025

M. Melzer, J. Chen, A. Heidenreich, J. Gab, M. Koller et al., Reversed Enantioselectivity of Diisopropyl Fluorophosphatase against Organophosphorus Nerve Agents by Rational Design, Journal of the American Chemical Society, vol.131, issue.47, pp.17226-17232, 2009.
DOI : 10.1021/ja905444g

M. Blum and J. Chen, Structural characterization of the catalytic calcium-binding site in diisopropyl fluorophosphatase (DFPase)???Comparison with related ??-propeller enzymes, Chemico-Biological Interactions, vol.187, issue.1-3, pp.373-379, 2010.
DOI : 10.1016/j.cbi.2010.02.043

C. Chen, K. Chin, A. Wang, and S. Chou, The First Crystal Structure of Gluconolactonase Important in the Glucose Secondary Metabolic Pathways, Journal of Molecular Biology, vol.384, issue.3, pp.604-614, 2008.
DOI : 10.1016/j.jmb.2008.09.055

N. Hansen and P. Coppens, Testing aspherical atom refinements on small-molecule data sets, Acta Crystallographica Section A, vol.34, issue.6, pp.909-921, 1978.
DOI : 10.1107/S0567739478001886

B. Zarychta, V. Pichon-pesme, B. Guillot, C. Lecomte, and C. Jelsch, On the application of an experimental multipolar pseudo-atom library for accurate refinement of small-molecule and protein crystal structures, Acta Crystallographica Section A Foundations of Crystallography, vol.63, issue.2, pp.108-125, 2007.
DOI : 10.1107/S0108767306053748/sh5051sup1.pdf

URL : https://hal.archives-ouvertes.fr/hal-00204860

D. Tronrud, C. Tnt-refinement-package-jr, and R. Sweet, Academic Press, In Macromolecular Crystallography Part B. Methods in Enzymology, vol.27797, issue.1997, pp.306-319

P. Emsley and K. Cowtan, : model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.2126-2132, 2004.
DOI : 10.1107/S0907444904019158

F. Allen, A systematic pairwise comparison of geometric parameters obtained by X-ray and neutron diffraction, Acta Crystallographica Section B Structural Science, vol.42, issue.5, pp.515-522, 1986.
DOI : 10.1107/S0108768186097823

H. Berman, K. Henrick, and H. Nakamura, Announcing the worldwide Protein Data Bank, Nature Structural & Molecular Biology, vol.277, issue.12, p.980, 2003.
DOI : 10.1016/S0076-6879(97)77032-0

P. Adams, P. Afonine, G. Bunkoczi, V. Chen, I. Davis et al., : a comprehensive Python-based system for macromolecular structure solution, Acta Crystallographica Section D Biological Crystallography, vol.64, issue.2, pp.213-221, 2010.
DOI : 10.1107/S0907444909052925

. Elias, Hydrogen atoms in protein structures: high-resolution X-ray diffraction structure of the DFPase, BMC Research Notes, vol.6, issue.1, p.308, 2013.
DOI : 10.1107/S0108768110007202

URL : https://hal.archives-ouvertes.fr/hal-01521944