?. Harrigan, P. Trentham, and D. , Kinetic studies of the acylation of pig muscle???d-glyceraldehyde 3-phosphate dehydrogenase by 1,3-diphosphoglycerate and of proton uptake and release in the overall enzyme mechanism, Biochemical Journal, vol.135, issue.4, pp.695-703, 1973.
DOI : 10.1042/bj1350695

?. Harrigan, P. Trentham, and D. , Kinetic studies of oxidized nicotinamide???adenine dinucleotide-facilitated reactions of d-glyceraldehyde 3-phosphate dehydrogenase, Biochemical Journal, vol.143, issue.2, pp.353-63, 1974.
DOI : 10.1042/bj1430353

D. R. Trentham, Reactions of d-glyceraldehyde 3-phosphate dehydrogenase facilitated by oxidized nicotinamide???adenine dinucleotide, Biochemical Journal, vol.122, issue.1, pp.59-69, 1971.
DOI : 10.1042/bj1220059

D. R. Trentham, Rate-determining processes and the number of simultaneously active sites of d-glyceraldehyde 3-phosphate dehydrogenase, Biochemical Journal, vol.122, issue.1, pp.71-77, 1971.
DOI : 10.1042/bj1220071

A. Soukri, A. Mougin, C. Corbier, A. Wonacott, C. Branlant et al., Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis, Biochemistry, vol.28, issue.6, pp.2586-2592, 1989.
DOI : 10.1021/bi00432a036

S. Michels, E. Rogalska, and G. Branlant, Phosphate-binding Sites in Phosphorylating glyceraldehyde-3-phosphate Dehydrogenase from Bacillus stearothermophilus, European Journal of Biochemistry, vol.84, issue.3, pp.641-647, 1996.
DOI : 10.1107/S0021889891004399

F. Talfournier, N. Colloc-'h, J. P. Mornon, and G. Branlant, Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis, European Journal of Biochemistry, vol.252, issue.3, pp.447-457, 1998.
DOI : 10.1046/j.1432-1327.1998.2520447.x

S. Boschi-muller and G. Branlant, The Active Site of Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase Is Not Designed to Increase the Nucleophilicity of a Serine Residue, Archives of Biochemistry and Biophysics, vol.363, issue.2, pp.259-266, 1999.
DOI : 10.1006/abbi.1998.1080

URL : https://hal.archives-ouvertes.fr/hal-01690988

T. Skarzyn´skiskarzyn´ski, P. C. Moody, and A. J. Wonacott, Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 ?? resolution, Journal of Molecular Biology, vol.193, issue.1, pp.171-187, 1987.
DOI : 10.1016/0022-2836(87)90635-8

I. Korndörfer, B. Steipe, R. Huber, A. Tomschy, J. et al., The Crystal Structure of Holo-glyceraldehyde-3-phosphate Dehydrogenase from the Hyperthermophilic BacteriumThermotoga maritimaat 2.5 ?? Resolution, Journal of Molecular Biology, vol.246, issue.4, pp.511-521, 1995.
DOI : 10.1006/jmbi.1994.0103

H. Kim, I. K. Feil, C. L. Verlinde, P. H. Petra, and W. G. Hol, Crystal Structure of Glycosomal Glyceraldehyde-3-phosphate Dehydrogenase from Leishmania mexicana: Implications for Structure-Based Drug Design and a New Position for the Inorganic Phosphate Binding Site, Biochemistry, vol.34, issue.46, pp.14975-14986, 1995.
DOI : 10.1021/bi00046a004

C. Corbier, S. Michels, A. J. Wonacott, and G. Branlant, Characterization of the two anion-recognition sites of glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus by site-directed mutagenesis and chemical modification, Biochemistry, vol.33, issue.11, pp.3260-3265, 1994.
DOI : 10.1021/bi00177a017

C. Didierjean, C. Corbier, M. Fatih, F. Favier, S. Boschi-muller et al., with NAD and d-Glyceraldehyde 3-Phosphate, Journal of Biological Chemistry, vol.254, issue.15, pp.12968-12976, 2003.
DOI : 10.1111/j.1432-1033.1978.tb12042.x

URL : https://hal.archives-ouvertes.fr/hal-01690824

A. R. Pearson, A. Mozzarelli, and G. L. Rossi, Microspectrophotometry for structural enzymology, Current Opinion in Structural Biology, vol.14, issue.6, pp.656-662, 2004.
DOI : 10.1016/j.sbi.2004.10.007

G. L. Rossi and S. A. Bernhard, On the relationship between the conformation and the catalyzed reactivity of acyl-chymotrypsin, Journal of Molecular Biology, vol.55, issue.2, pp.215-230, 1971.
DOI : 10.1016/0022-2836(71)90193-8

A. Mozzarelli and G. L. Rossi, Protein Function in the Crystal, Annual Review of Biophysics and Biomolecular Structure, vol.25, issue.1, pp.343-365, 1996.
DOI : 10.1146/annurev.bb.25.060196.002015

D. Bourgeois and A. Royant, Advances in kinetic protein crystallography, Current Opinion in Structural Biology, vol.15, issue.5, pp.538-547, 2005.
DOI : 10.1016/j.sbi.2005.08.002

R. Berni, A. Mozzarelli, L. Pellacani, and G. L. Rossi, Catalytic and regulatory properties of d-glyceraldehyde-3-phosphate dehydrogenase in the crystal, Journal of Molecular Biology, vol.110, issue.2, pp.405-415, 1977.
DOI : 10.1016/S0022-2836(77)80079-X

W. Kabsch, Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants, Journal of Applied Crystallography, vol.26, issue.6, pp.795-800, 1993.
DOI : 10.1107/S0021889893005588

A. Vagin and A. Teplyakov, : an Automated Program for Molecular Replacement, Journal of Applied Crystallography, vol.30, issue.6, pp.1022-1025, 1997.
DOI : 10.1107/S0021889897006766

G. N. Murshudov, A. A. Vagin, and E. J. Dodson, Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.3, pp.240-255, 1997.
DOI : 10.1107/S0907444996012255

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

R. A. Laskowski, M. W. Macarthur, D. S. Moss, T. , and J. M. , PROCHECK: a program to check the stereochemical quality of protein structures, Journal of Applied Crystallography, vol.26, issue.2, pp.283-291, 1993.
DOI : 10.1107/S0021889892009944

C. Ramakrishnan and G. N. Ramachandran, Stereochemical Criteria for Polypeptide and Protein Chain Conformations, Biophysical Journal, vol.5, issue.6, pp.909-933, 1965.
DOI : 10.1016/S0006-3495(65)86759-5

E. Duée, L. Olivier-deyris, E. Fanchon, C. Corbier, G. Branlant et al., Comparison of the Structures of Wild-type and a N313T Mutant ofEscherichia coliGlyceraldehyde 3-Phosphate Dehydrogenases: Implication for NAD Binding and Cooperativity, Journal of Molecular Biology, vol.257, issue.4, pp.814-838, 1996.
DOI : 10.1006/jmbi.1996.0204

P. J. Harrigan and D. R. Trentham, Kinetic studies of oxidized nicotinamide???adenine dinucleotide-facilitated reactions of d-glyceraldehyde 3-phosphate dehydrogenase, Biochemical Journal, vol.143, issue.2, pp.353-363, 1974.
DOI : 10.1042/bj1430353

M. Buehner, G. C. Ford, D. Moras, K. W. Olsen, and M. G. And-rossmann, Structure determination of crystalline lobster d-glyceraldehyde-3-phosphate dehydrogenase, Journal of Molecular Biology, vol.82, issue.4, pp.563-585, 1974.
DOI : 10.1016/0022-2836(74)90249-6

L. D. Byers, Enantiomeric specificity of glyceraldehyde 3-phosphate dehydrogenase, Archives of Biochemistry and Biophysics, vol.186, issue.2, pp.335-342, 1978.
DOI : 10.1016/0003-9861(78)90443-5

D. Cobessi, F. Tête-favier, S. Marchal, G. Branlant, A. et al., Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans, Journal of Molecular Biology, vol.300, issue.1, pp.141-152, 2000.
DOI : 10.1006/jmbi.2000.3824

URL : https://hal.archives-ouvertes.fr/hal-00151125

?. Ahn, S. Moniot, S. Elias, M. Chabriere, E. Kim et al., Structure-function relationships in a bacterial DING protein, FEBS Letters, vol.42, issue.18, pp.3455-60, 2007.
DOI : 10.1016/S0163-7827(03)00015-8

?. Belenky, M. Prasain, J. Kim, H. Barnes, and S. , DING, a Genistein Target in Human Breast Cancer: A Protein Without a Gene, The Journal of Nutrition, vol.19, issue.suppl. 3, pp.2497-2501, 2003.
DOI : 10.1038/sj.onc.1203273

?. Berna, A. Bernier, F. Chabriere, E. Perera, T. Scott et al., DING proteins; novel members of a prokaryotic phosphate-binding protein superfamily which extends into the eukaryotic kingdom, The International Journal of Biochemistry & Cell Biology, vol.40, issue.2, pp.170-175, 2008.
DOI : 10.1016/j.biocel.2007.02.004

URL : https://hal.archives-ouvertes.fr/hal-00255777

?. Berna, A. Bernier, F. Scott, K. Stuhlmuller, and B. , Ring up the curtain on DING proteins, FEBS Letters, vol.8, issue.1-3, pp.6-10, 2002.
DOI : 10.1016/S0962-8924(98)01362-2

?. Chang, G. Roth, and C. B. , Structure of MsbA from E. coli: A Homolog of the Multidrug Resistance ATP Binding Cassette (ABC) Transporters, Science, vol.293, issue.5536, pp.1793-1800, 2001.
DOI : 10.1126/science.293.5536.1793

?. Darbinian-sarkissian, N. Darbinyan, A. Otte, J. Radhakrishnan, S. Sawaya et al., p27SJ, a novel protein in St John's Wort, that suppresses expression of HIV-1 genome, Gene Therapy, vol.160, issue.Suppl A, pp.288-295, 2003.
DOI : 10.1126/science.160.3826.421

?. Diemer, H. Elias, M. Renault, F. Contreras-martel, C. Schaeffer et al., Tandem use of X-ray crystallography and mass spectrometry to obtain ab initio the complete and exact amino acids sequence of HPBP, a human 38-kDa apolipoprotein, Proteins: Structure, Function, and Bioinformatics, vol.53, issue.Part 3, pp.1708-1728, 2008.
DOI : 10.1042/bj2300353

?. Fokine, A. Morales, R. Contreras-martel, C. Carpentier, P. Renault et al., Direct phasing at low resolution of a protein copurified with human paraoxonase (PON1), Acta Crystallographica Section D Biological Crystallography, vol.59, issue.12, pp.2083-2087, 2003.
DOI : 10.1107/S0907444903017682

?. Luecke, H. Quiocho, and F. A. , High specificity of a phosphate transport protein determined by hydrogen bonds, Nature, vol.347, issue.6291, pp.402-406, 1990.
DOI : 10.1038/347402a0

?. Renault, F. Chabriere, E. Andrieu, J. P. Dublet, B. Masson et al., Tandem purification of two HDL-associated partner proteins in human plasma, paraoxonase (PON1) and phosphate binding protein (HPBP) using hydroxyapatite chromatography, Journal of Chromatography B, vol.836, issue.1-2, pp.15-21, 2006.
DOI : 10.1016/j.jchromb.2006.03.029

URL : https://hal.archives-ouvertes.fr/hal-00204670

?. Scott, K. Wu, and L. , Functional properties of a recombinant bacterial DING protein: Comparison with a homologous human protein, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1744, issue.2, pp.234-244, 2005.
DOI : 10.1016/j.bbamcr.2005.02.003

M. Belenky, J. Prasain, H. Kim, and S. Barnes, DING, a Genistein Target in Human Breast Cancer: A Protein Without a Gene, The Journal of Nutrition, vol.19, issue.suppl. 3, pp.2497-2501, 2003.
DOI : 10.1038/sj.onc.1203273

A. Berna, F. Bernier, K. Scott, and B. Stuhlmuller, Ring up the curtain on DING proteins, FEBS Letters, vol.8, issue.1-3, pp.6-10, 2002.
DOI : 10.1016/S0962-8924(98)01362-2

Z. Chen, C. F. Franco, R. P. Baptista, J. M. Cabral, A. V. Coelho et al., Purification and identification of cutinases from Colletotrichum kahawae and Colletotrichum gloeosporioides, Applied Microbiology and Biotechnology, vol.18, issue.18, pp.1306-1313, 2007.
DOI : 10.1007/s00253-006-0605-1

N. Darbinian-sarkissian, A. Darbinyan, J. Otte, S. Radhakrishnan, B. E. Sawaya et al., p27SJ, a novel protein in St John's Wort, that suppresses expression of HIV-1 genome, Gene Therapy, vol.160, issue.Suppl A, pp.288-295, 2006.
DOI : 10.1126/science.160.3826.421

M. Du, L. Zhao, C. Li, G. Zhao, and X. Hu, Purification and characterization of a novel fungi Se-containing protein from Se-enriched Ganoderma Lucidum mushroom and its Se-dependent radical scavenging activity, European Food Research and Technology, vol.524, issue.5, pp.659-665, 2007.
DOI : 10.1016/S0925-4439(01)00104-1

J. Jancarik and S. Kim, Sparse matrix sampling: a screening method for crystallization of proteins, Journal of Applied Crystallography, vol.24, issue.4, pp.409-411, 1991.
DOI : 10.1107/S0021889891004430

W. Kabsch, Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants, Journal of Applied Crystallography, vol.26, issue.6, pp.795-800, 1993.
DOI : 10.1107/S0021889893005588

V. Kumar, S. Yu, G. Farell, F. G. Toback, and J. C. Lieske, Renal epithelial cells constitutively produce a protein that blocks adhesion of crystals to their surface, American Journal of Physiology-Renal Physiology, vol.287, issue.3, pp.373-383, 2004.
DOI : 10.1046/j.1523-1755.2001.059002637.x

H. Luecke and F. A. Quiocho, High specificity of a phosphate transport protein determined by hydrogen bonds, Nature, vol.347, issue.6291, pp.402-406, 1990.
DOI : 10.1038/347402a0

B. W. Matthews, Solvent content of protein crystals, Journal of Molecular Biology, vol.33, issue.2, pp.491-497, 1968.
DOI : 10.1016/0022-2836(68)90205-2

R. Morales, Serendipitous Discovery and X-Ray Structure of a Human Phosphate Binding Apolipoprotein, Structure, vol.14, issue.3, pp.601-609, 2006.
DOI : 10.1016/j.str.2005.12.012

URL : https://hal.archives-ouvertes.fr/hal-00093028

K. Scott and L. Wu, Functional properties of a recombinant bacterial DING protein: Comparison with a homologous human protein, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1744, issue.2, pp.234-244, 2005.
DOI : 10.1016/j.bbamcr.2005.02.003

N. K. Vyas, N. M. Vyas, and F. A. Quiocho, Crystal Structure of M. tuberculosis ABC Phosphate Transport Receptor, Structure, vol.11, issue.7, pp.765-774, 2003.
DOI : 10.1016/S0969-2126(03)00109-6

W. K. Weebadda, G. J. Hoover, D. B. Hunter, and M. A. Hayes, Avian air sac and plasma proteins that bind surface polysaccharides of Escherichia coli O2, Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, vol.130, issue.3, pp.299-312, 2001.
DOI : 10.1016/S1096-4959(01)00432-8

A. Berna, F. Bernier, K. Scott, and B. Stuhlmuller, Ring up the curtain on DING proteins, Mean I/(I) 38.9 (10.52) References [1], pp.6-10, 2002.
DOI : 10.1016/S0962-8924(98)01362-2

A. Berna, F. Bernier, E. Chabriere, T. Perera, and K. Scott, in press) DING proteins; novel members of a prokaryotic phosphate-binding protein superfamily which extends into the Eukaryotic Kingdom, Intl. J. Biochem. Cell Biol. Feb, 2007.

A. Fokine, R. Morales, C. Contreras-martel, P. Carpentier, F. Renault et al., Direct phasing at low resolution of a protein copurified with human paraoxonase (PON1), Acta Crystallographica Section D Biological Crystallography, vol.59, issue.12, pp.2083-2087, 2003.
DOI : 10.1107/S0907444903017682

F. Renault, E. Chabriere, J. P. Andrieu, B. Dublet, P. Masson et al., Tandem purification of two HDL-associated partner proteins in human plasma, paraoxonase (PON1) and phosphate binding protein (HPBP) using hydroxyapatite chromatography, Journal of Chromatography B, vol.836, issue.1-2, pp.15-21, 2006.
DOI : 10.1016/j.jchromb.2006.03.029

URL : https://hal.archives-ouvertes.fr/hal-00204670

R. Morales, A. Berna, P. Carpentier, C. Contreras-martel, F. Renault et al., Serendipitous Discovery and X-Ray Structure of a Human Phosphate Binding Apolipoprotein, Structure, vol.14, issue.3, pp.601-609, 2006.
DOI : 10.1016/j.str.2005.12.012

URL : https://hal.archives-ouvertes.fr/hal-00093028

H. Diemer, M. Elias, F. Renault, C. Contreras-martel, C. Schaeffer et al., preparation ) Tandem use of X-ray crystallography and mass spectrometry to obtain ab initio the complete and exact amino acids sequence of HPBP

H. Luecke and F. A. Quiocho, High specificity of a phosphate transport protein determined by hydrogen bonds, Nature, vol.347, issue.6291, pp.402-406, 1990.
DOI : 10.1038/347402a0

G. Chang and C. B. Roth, Structure of MsbA from E. coli: A Homolog of the Multidrug Resistance ATP Binding Cassette (ABC) Transporters, Science, vol.293, issue.5536, pp.1793-1800, 2001.
DOI : 10.1126/science.293.5536.1793

K. Scott and L. Wu, Functional properties of a recombinant bacterial DING protein: Comparison with a homologous human protein, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1744, issue.2, pp.234-244, 2005.
DOI : 10.1016/j.bbamcr.2005.02.003

N. A. Hain, B. Stuhlmuller, G. R. Hahn, J. R. Kalden, R. Deutzmann et al., Biochemical characterisation and microsequencing of a 205 kDa synovial protein stimulatory for T cells and reactive with rheumatoid factor containing sera, J. Immunol, vol.157, pp.1773-1780, 1996.

D. Bush, H. Fritz, C. Knight, J. Mount, and K. Scott, A hirudin-sensitive, growth-related proteinase from human fibroblasts, Biol. Chem, vol.379, pp.225-229, 1998.

L. Adams, S. Davey, and K. Scott, The DING protein: an autocrine growth-stimulatory protein related to the human synovial stimulatory protein, Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, vol.1586, issue.3, pp.254-264, 2002.
DOI : 10.1016/S0925-4439(01)00104-1

M. Belenky, J. Prasain, H. Kim, and S. Barnes, DING, a Genistein Target in Human Breast Cancer: A Protein Without a Gene, The Journal of Nutrition, vol.19, issue.suppl. 3, 2003.
DOI : 10.1038/sj.onc.1203273

S. Moniot, M. Elias, D. Kim, K. Scott, and E. Chabriere, press) Crystallization, diffraction data collection and preliminary crystallographic analysis of DING protein from Pseudomonas fluorescens, Acta Cryst. F, vol.63, pp.1-3

A. Vagin and A. Teplyakov, : an Automated Program for Molecular Replacement, Journal of Applied Crystallography, vol.30, issue.6, pp.1022-1025, 1997.
DOI : 10.1107/S0021889897006766

G. N. Murshudov, A. A. Vagin, and E. J. Dodson, Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.3, pp.240-255, 1997.
DOI : 10.1107/S0907444996012255

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

L. J. Mcguffin, K. Bryson, and D. T. Jones, The PSIPRED protein structure prediction server, Bioinformatics, vol.16, issue.4, pp.404-405, 2000.
DOI : 10.1093/bioinformatics/16.4.404

S. N. Ho, H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease, Site-directed mutagenesis by overlap extension using the polymerase chain reaction, Gene, vol.77, issue.1, pp.51-59, 1989.
DOI : 10.1016/0378-1119(89)90358-2

R. Tam and M. H. Saier, Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria, Microbiol. Rev, vol.57, pp.320-346, 1993.

C. B. Felder, R. C. Graul, A. Y. Lee, H. P. Merkle, and W. Sadee, The venus flytrap of periplasmic binding proteins: An ancient protein module present in multiple drug receptors, AAPS PharmSci, vol.1, issue.2, 1999.
DOI : 10.1208/ps010202

K. Poole and R. E. Hancock, Phosphate transport in Pseudomonas aeruginosa. Involvement of a periplasmic phosphate-binding protein, European Journal of Biochemistry, vol.160, issue.3, pp.607-612, 1984.
DOI : 10.1016/0003-2697(81)90179-2

Z. Wang, A. Choudhary, P. S. Ledvina, and F. A. Quiocho, Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-directed mutagenesis, ligand binding, and crystallographic studies, J. Biol. Chem, vol.269, pp.25091-25094, 1994.

K. Watterson, S. Sankala, S. Milstien, and S. Spiegel, Pleiotropic actions of sphingosine-1-phosphate, Progress in Lipid Research, vol.42, issue.4, pp.344-357, 2003.
DOI : 10.1016/S0163-7827(03)00015-8