199-l) Cn'stallogr<lphic study of coenzyme , coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for ADP specificit:· ilnd the enzyme mechanism. StI"llCtll, pp.651-668 ,
Structure of trypanothione reductase from Crithidia fasciculata at 2.6 ?? resolution; enzyme???NADP interactions at 2.8 ?? resolution, Acta Crystallographica Section D Biological Crystallography, vol.50, issue.2, pp.139-154, 1992. ,
DOI : 10.1107/S0907444993011898
0175 discriminates bet\\'een NADH and NADPH in the coenzyme binding site of Lactobacil- llis riclbrucckii subsp. blilgariClls D-Iactate dehydrogenase, Biocllelll. Biopliys. Res. COli1111lin, vol.208, pp.895-900, 1995. ,
The protein data bank: A computer-based archival file for macromolecular structures, Journal of Molecular Biology, vol.112, issue.3, pp.535-540 ,
DOI : 10.1016/S0022-2836(77)80200-3
Sequence and structure of Dglyceraldehyde 3-phosphate dehydrogenase from Bacil, pp.328-333 ,
Crystal structures of Escliaicliia wli and Lllclo!>llcil/lii cnsci dihl'drnfal,lte reductas !:' refined ilt 1.7 A resolutiOli. 1. General feiltmes ilnd binding of methotrexate. f, Clielll, vol.257, pp.13630-13662, 1982. ,
Recognition of different nucleotide-binding sites in primary structures using a property-pattern ilpproach, Elir. f. Biocli,'III, vol.191, pp.3-7, 1990. ,
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures, Nalllre, vol.355, pp.472-475, 1992. ,
X-PLOR Manllal, pasion 3, 1992. ,
Crystallographic R Factor Refinement by Molecular Dynamics, Science, vol.235, issue.4787, pp.458-460, 1987. ,
DOI : 10.1126/science.235.4787.458
Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenase, Journal of Molecular Biology, vol.90, issue.1, pp.25-49 ,
DOI : 10.1016/0022-2836(74)90254-X
Crystal structures of Eselleriellia coli dihydrofolate reductase: the NADP+ holoènzyme and the folate-NADP-ternary complex. 5ubstrate binding and a model for the transition state, Biocllclllislnf, vol.29, pp.3263-3295, 1990. ,
Glyceraldehyde-3-phosphate dehydrogenase ( ADP) from Sinal'is all1l1 L. NAD(P)induced conformation changes of the enzyme, Elir. f. BiocllCl/I, vol.82, pp.5-53, 1978. ,
Quaternilry structure of higher plant glyceraldehyde-3-phosphate dehydrogenases, 1979. ,
CH/?? Interaction in the Packing of the Adenine Ring in Protein Structures, Journal of Molecular Biology, vol.251, issue.1, pp.9-10, 1995. ,
DOI : 10.1006/jmbi.1995.0411
199-!).· The structure of PncllllloCifstis cnrinii dihl, pp.915-92 ,
A highly active decarboxylating deh:'drogenase \\'ith rationally inverted coenzyme specificity, Proc. I\'all ACrld, pp.11666-11670, 1995. ,
Role of -aspartic acid 38 in the cofactor specificity of Oros,lphila alcohol dehydrogenase. Ellr. f. BÙ1c!lelll, pp.263-267, 1991. ,
H. (199-!) Adding a positil'e ch<lrge ilt residue -l6 of Orosophila alcohol dehydrogenase increases cofactor specificity for NADP-. FEBS Lellers, pp.81-83 ,
URL : https://hal.archives-ouvertes.fr/in2p3-00024976
Detennimnts of coenzyme specificity in glyceraldehyde-3-phosphilte dehydrogenase: role of the acidic residue in the fingerprint region of the nucleotide binding fold, pp.10178-1018, 1993. ,
Cn'stal structure determination at 2.3 À of recombin;nt human dihnirofoI,lte reductase ternary complex with NADPH ;lI1d methotrexate-·f-tetrazole . Allti-CflIlCt, pp.3-91, 1992. ,
The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis, Biochimie, vol.72, pp.545-554, 1990. ,
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
Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications, pp.859-868, 1994. ,
Structure of porcine aldehyde reductase holoenzyme, Nature Structural Biology, vol.4, issue.8, pp.687-692, 1995. ,
DOI : 10.1016/0168-9002(94)90720-X
Accurate bond and angle parameters for X-ray protein structure refinement, Acta Crystallographica Section A Foundations of Crystallography, vol.47, issue.4, pp.392-400, 1991. ,
DOI : 10.1107/S0108767391001071
Phosphor- ous-31 nuclear magnetic resonance studies on coenzyme binding and specificity in glyceraldehyde-3- phosphate dehydrogenase, Biochemistry, vol.35, pp.606-6072, 1996. ,
An aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme, Biochemistry, vol.30, issue.26, pp.6397-6401, 1991. ,
DOI : 10.1021/bi00240a008
Subunit structure and activity of glyceraldehyde-3-phosphate dehydrogenase from spinach chloroplasts, Biochimica et Biophysica Acta (BBA) - Enzymology, vol.522, issue.1, pp.19-31, 1978. ,
DOI : 10.1016/0005-2744(78)90318-2
Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.1041, issue.1, pp.36-42, 1990. ,
DOI : 10.1016/0167-4838(90)90119-Z
Crystal structures of Escherichia coli and Lactobacil/lis cast'i dihydrofolate reductase refined at 1.7 À resolution. II. Environment of bound NADPH and implications for catalysis, J. Biol. Chell, vol.257, pp.13663-13672, 1982. ,
The NADPH binding site on beef liver catalase., Proc. Nat! Acad. Sci. USA, pp.1604-1608, 1985. ,
DOI : 10.1073/pnas.82.6.1604
Crystal Structure ofProteus mirabilisPR Catalase With and Without Bound NADPH, Journal of Molecular Biology, vol.249, issue.5, pp.933-954, 1995. ,
DOI : 10.1006/jmbi.1995.0350
Characterization of nucleoti'de binding properties of a mutant dihydropteridine reductase containing an aspartate 37- isoleucine replacement, J. Biol. Chelll, vol.267, pp.15334-15339, 1992. ,
Importance of lysine-286 at the NADP site of glutamilte dehydrogenase from Sallllollel/II typhilllllrilllll, pp.7807-7814, 1992. ,
cDNA sequence of adrenodoxin reductilse. Identification of NADPbinding sites in oxidoreductases, Elir. J. Biochelll, vol.1, issue.180, pp.479-484, 1989. ,
Helix stop signais in proteins and peptides: the capping box, Biachelllistry, vol.32, pp.7605-7609, 1993. ,
Glyceraldehyde-3-phos- phate dehydrogenase, pp.1-49, 1976. ,
Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily., Proc. Natl Acad. Sci. USA, pp.2517-2521, 1994. ,
DOI : 10.1073/pnas.91.7.2517
Role of l\'sine-54 in determining cofactor specificity and llinding in human dihydrofolate reductase, Biocllcllli, vol.29, pp.8063-8069, 1990. ,
Structure of 3-iso- propylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity, pp.1007-1016, 1994. ,
Catal\·tic mechanism of \:ADP-dependent isocitrate' deh~'drogen,lse: implications from the structures of magnesium-isocitrate and NADP+ complexes, Biochclllistry, vol.30, pp.8671-8677, 1991. ,
haluation of single-crystal \-ray diffraction data from a position-sensiti\'e detector, 1988. ,
Automatic processing of rotation diffraction data from cr\'stals of initiall\' unknown symmetry and cell con~tants, J. Appl. 6ysttllh1g, vol.26, pp.795-800, 1993. ,
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
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
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, Journal of Applied Crystallography, vol.24, issue.5, pp.946-950, 1991. ,
DOI : 10.1107/S0021889891004399
Site-directed mutagenesis of a serine residue in cinnamd alcohol dehydrogenase, il plant l\.-\DPH-depend~nt dehydrogenase , affects the specificit\, for the coenzvme, Biachelllistry, vol.34, pp.12426-12434, 1995. ,
i\:AD-binding dnm,lins of dehydrogenases. CII/T. 0l'ill, Stmct. Bin, vol.5, pp.5-783 ,
Coenz\'n11' binding in cryst,lls of gl\'ceI"1Idelwde-3-phospha te dehydrogenase, Mol. Bin, vol.165, issue.1, pp.3-391, 1983. ,
Identification of an Arginine Residue in the Dual Coenzyme-Specific Glucose-6-Phosphate Dehydrogenase fromLeuconostoc mesenteroidesThat Plays a Key Role in Binding NADP+but Not NAD+, Archives of Biochemistry and Biophysics, vol.326, issue.1, pp.145-151, 1996. ,
DOI : 10.1006/abbi.1996.0058
Structure of D-Glyceraldehyde-3-Phosphate Dehydrogenase from Palinurus versicolor Carrying the Fluorescent NAD Derivatives at 2.7?? Resolution, Archives of Biochemistry and Biophysics, vol.302, issue.1, pp.161-166, 1993. ,
DOI : 10.1006/abbi.1993.1194
Prokaryotic features of a nucleus-encoded enzyme. cDNA sequences for chloroplast and cytosolic glyceraldehyde-3-phos- phate dehydrogenases from mustard, 1986. ,
New flavoenzymes, Current Opinion in Structural Biology, vol.1, issue.6, pp.954-967, 1991. ,
DOI : 10.1016/0959-440X(91)90091-7
Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin, Biochemistry, vol.31, issue.32, pp.7264-7273, 1992. ,
DOI : 10.1021/bi00147a009
Twinning in ctystals of human skeletal muscle D- glyceraldehyde-3-phosphate dehydrogenase, J. Mol, 1976. ,
Amino Acid Substitutions in the Yeast Pichia Stipitis Xylitol Dehydrogenase Coenzyme-Binding Domain Affect the Coenzyme Specificity, European Journal of Biochemistry, vol.187, issue.1, pp.50-54, 1995. ,
DOI : 10.1038/343038a0
Structure of glutathione reductase from Eseheriehia coli at 1.86 À resolution: comparison with the enzyme from human erythrocytes, pp.799-809, 1994. ,
Anatomy of an engineered NAD-binding site, Protein Science, vol.187, issue.9, pp.1504-1514, 1994. ,
DOI : 10.1042/bj2450875
HB8, "Protein Engineering, Design and Selection", vol.7, issue.3, pp.401-403, 1994. ,
DOI : 10.1093/protein/7.3.401
Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chem, vol.250, pp.9137-9162, 1975. ,
Use of site-directed mutagenesis to probe the role of Cys l-l9 in the formation of charge-transfer transition in glycer- aldehyde-3-phosphate dehydrogenase, pp.45-48, 1988. ,
Alteration of coenzyme specificity of malate dehydrogen- ase from Thermus flavus by site-directed mutagenesis, J. Biol. Chem, vol.268, pp.4656-4660, 1993. ,
Oscillation data reduction program, Proceedings of the CCP4 Stlldy Weekend: Data Collection and Processing, pp.56-62, 1993. ,
Variations on a theme: the family of FAD-dependent NAD(P)H-(disulphide)-oxidoreductases, Current Opinion in Structural Biology, vol.1, issue.5, pp.796-803, 1991. ,
DOI : 10.1016/0959-440X(91)90181-R
The mechanism of oxidation of aldehydes by glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chem, vol.198, pp.731-738, 1952. ,
Etude des facteurs moléculaires responsables de la spécificité de cofacteur des 123, 1994. ,
NAOpr Interactions with GAPOH Mutants déshydrogénases à NAD(P) Thèse d'Université ,
Molecular symmetry axes and subunit interfaces in certain dehydrogenases, Journal of Molecular Biology, vol.76, issue.4, pp.533-537, 1973. ,
DOI : 10.1016/0022-2836(73)90491-9
Chemical and biological evolution of a nucleotide-binding protein, Nature, vol.243, issue.5463, pp.194-199, 1974. ,
DOI : 10.1101/SQB.1972.036.01.032
2 Evolutionary and Structural Relationships among Dehydrogenases, Tize Enzymes, pp.61-102, 1975. ,
DOI : 10.1016/S1874-6047(08)60210-3
TURBO-FRODO. ln Silicoll Graphies Geometry Partller Direetory (Silicon graphics, pp.77-78, 1989. ,
Binding of nucleotides by proteins. Cil 1'1'. Opin, Struet. Biol, vol.2, pp.61-67, 1992. ,
Redesign of the coenzyme specificity of a dehydrogenase by protein
engineering, Nature, vol.343, issue.6253, pp.38-43, 1990. ,
DOI : 10.1038/343038a0
Sequence determinants of the capping box, a stabilizing motif at the N-termini of ??-helices, Protein Science, vol.31, issue.10, pp.1741-1745, 1994. ,
DOI : 10.1111/j.1399-3011.1993.tb00470.x
Enzyme-substrate binding interactions of NADPH-cytochrome P-450 oxidoreductase characterized with pH and alternate substrate/inhibitor studies, Biochemistry, vol.32, issue.43, pp.11539-11547, 1993. ,
DOI : 10.1021/bi00094a010
Interaction with arginine 597 of NADPH-cytochrome P-450 oxidoreductase is a prin1ary source of the uniform binding energy used to discrimina te between NADPH and NADH, Biocllel1listry, vol.32, pp.11548-11558, 1993. ,
Evidence in favor of the symbiotic origin of chloroplasts: Primary structure and evolution of tobacco glyceraldehyde-3-phosphate dehydrogenases, Cell, vol.47, issue.1, pp.73-80, 1986. ,
DOI : 10.1016/0092-8674(86)90367-3
Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus, Journal of Molecular Biology, vol.203, issue.4, pp.1097-1118, 1988. ,
DOI : 10.1016/0022-2836(88)90130-1
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
Structure of isocitrate dehydrogenase with isocitrate , nicotinamide ?denine dinucleotide phosphilte, and calcium at 2.5 A resolution: a pseudo-Michaelis temary complex, Bioclleillislry, vol.32, pp.9310-9316, 1993. ,
Bioehel1listry, 4th edit, 1995. ,
Waterinserted ~-helical segments implicate reverse turns as folding interrnediates, Science, vol.244, pp.1333-1337, 1989. ,
Determinants of enzyme thermostability observed in the molecular structure of Therl11us aquatiClis D-glyceral- dehyde-3-phosphate dehydrogenase at' 2:5 À resolution, Biochel11istry, vol.35, pp.2597-2609, 1996. ,
Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH. f, Mol. Biol, vol.249, pp.785-799, 1995. ,
Prediction of the occurrence of the ADP-binding ??????-fold in proteins, using an amino acid sequence fingerprint, Journal of Molecular Biology, vol.187, issue.1, pp.101-107, 1986. ,
DOI : 10.1016/0022-2836(86)90409-2
An unlikely sugar substrate site in the 1, 1992. ,
isocitrate dehydrogenase in the coenzyme specificity, FEBS Letters, vol.221, issue.2, pp.171-172 ,
DOI : 10.1111/j.1432-1033.1994.tb18805.x
Receiven 11 DecelJlber 1996; receÎl'ed il1 rCï.'ised forlJl 1ï Fell/ïm}'!! 199ï ,
Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism, Structure, vol.2, issue.7, pp.651-668, 1994. ,
DOI : 10.1016/S0969-2126(00)00066-6
Structure of Lactate Dehydrogenase at 2.8 ?? Resolution, Nature, vol.245, issue.5263, pp.1098-1103, 1970. ,
DOI : 10.1515/bchm2.1969.350.1.28
The crystallization and properties of glyceraldehyde-3-phosphate dehydrogenase isolated from rabbit muscle by a simplified procedure, Biochimica et Biophysica Acta (BBA) - Enzymology, vol.132, issue.2, pp.256-259 ,
DOI : 10.1016/0005-2744(67)90144-1
Imaging plate illuminates many fields, Nature, vol.336, issue.6194, pp.89-90 ,
DOI : 10.1038/336089a0
The optimum strategy in measuring structure factors, Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry, vol.24, issue.10, pp.1355-1357 ,
DOI : 10.1107/S0567740868004292
Structure of trypanothione reductase from Crithidia fasciculata at 2.6 ?? resolution; enzyme???NADP interactions at 2.8 ?? resolution, Acta Crystallographica Section D Biological Crystallography, vol.50, issue.2, pp.139-154 ,
DOI : 10.1107/S0907444993011898
Structural consequences of sequence patterns in the fingerprint region of the nuc\eotide binding fold ,
D175 Discriminates Between NADH and NADPH in the Coenzyme Binding Site of Lactobacillus delbrueckii subsp. Bulgaricus D-Lactate Dehydrogenase, Biochemical and Biophysical Research Communications, vol.208, issue.3, pp.895-900, 1995. ,
DOI : 10.1006/bbrc.1995.1419
Crystallographic symmetry and coenzyme binding properties of D-glyceraldehyde-3-phosphate dehydrogenase from the tail muscle of PalillUTUS vulgaris, J. Biol. Chem, vol.254, pp.8004-8006, 1979. ,
The protein data bank: A computer-based archival file for macromolecular structures, Journal of Molecular Biology, vol.112, issue.3, pp.535-542, 1977. ,
DOI : 10.1016/S0022-2836(77)80200-3
Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus, Nature, vol.69, issue.5600, pp.328-333, 1977. ,
DOI : 10.1042/bj1190805f
Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering, Biochemistry, vol.32, issue.11, pp.2737-2740, 1993. ,
DOI : 10.1021/bi00062a001
Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Â resolution. 1. General features and binding of methotrexate, J. Biol. Chem, vol.257, pp.13650-13662, 1982. ,
Recognition of different nucleotide-binding sites in primary structures using a property-pattern approach, European Journal of Biochemistry, vol.26, issue.2, pp.347-358, 1990. ,
DOI : 10.1038/343038a0
Crystallographic R Factor Refinement by Molecular Dynamics, Science, vol.235, issue.4787, pp.458-460, 1987. ,
DOI : 10.1126/science.235.4787.458
Crystallographic refinement by simulated annealing: application to crambin, Acta Crystallographica Section A Foundations of Crystallography, vol.45, issue.1, pp.50-61, 1989. ,
DOI : 10.1107/S0108767388009195
Slow-cooling protocols for crystallographic refinement by simulated annealing, Acta Crystallographica Section A Foundations of Crystallography, vol.46, issue.7, pp.585-593, 1990. ,
DOI : 10.1107/S0108767390002355
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures, Nature, vol.355, issue.6359, pp.472-475, 1992. ,
DOI : 10.1038/355472a0
X-PLOR Mallual, version 3 ,
Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenase, Journal of Molecular Biology, vol.90, issue.1, pp.25-49, 1974. ,
DOI : 10.1016/0022-2836(74)90254-X
Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate .cntdot. NADP+ ternary complex. substrate binding and a model for the transition state, Biochemistry, vol.29, issue.13, pp.3263-3277, 1990. ,
DOI : 10.1021/bi00465a018
Cold Sprillg Harbor Symp, Quant. Biol, vol.36, pp.165-170, 1971. ,
Glyceraldehyde-3-Phosphate Dehydrogenase(NADP) from Sinapis alba L.. NAD(P)-Induced Conformation Changes of the Enzyme, European Journal of Biochemistry, vol.87, issue.1, pp.45-53, 1978. ,
DOI : 10.1016/0003-9861(64)90184-5
Quaternary Structure of Higher Plant Glyceraldehyde-3-Phosphate Dehydrogenases, European Journal of Biochemistry, vol.61, issue.1, pp.243-247, 1979. ,
DOI : 10.1016/0003-9861(73)90064-7
CHl1t interaction in the packing of the adenine ring in protein structures, 1995. ,
The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 ?? resolution, Structure, vol.2, issue.10, pp.915-924, 1994. ,
DOI : 10.1016/S0969-2126(94)00093-X
A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity., Proc. Natl. Acad. Sci. 92, pp.1666-11670, 1995. ,
DOI : 10.1073/pnas.92.25.11666
Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase, European Journal of Biochemistry, vol.24, issue.2, pp.263-267, 1991. ,
DOI : 10.1016/0167-4838(82)90125-X
Determinants of coenzyme specificity in glyceraldehyde-3-phosphate dehydrogenase: Role of the acidic residue in the fingerprint region of the nucleotide binding fold, Biochemistry, vol.32, issue.38, pp.10178-10184, 1993. ,
DOI : 10.1021/bi00089a038
URL : https://hal.archives-ouvertes.fr/hal-01652822
Crystal structure determination at 2.3 À of recombinant human dihydrofolate reductase ternary complex with NADPH and methotrexate-y-tetrazole, 1992. ,
The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis, Biochimie, vol.72, issue.8, pp.545-554, 1990. ,
DOI : 10.1016/0300-9084(90)90119-2
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
A method of positioning a known molecule in an unknown crystal structure, Acta Crystallographica, vol.23, issue.4, pp.544-548, 1967. ,
DOI : 10.1107/S0365110X67003172
The fast rotation function, pp.173-178, 1972. ,
Protein precision re-exarnined : Luzzati plots do not estimate final errors, 1996. ,
Proteins at atomic resolution, Current Opinion in Structural Biology, vol.5, issue.6, pp.784-790, 1995. ,
DOI : 10.1016/0959-440X(95)80011-5
Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis, Science, vol.358, issue.6387, pp.1638-1641, 1995. ,
DOI : 10.1038/358591a0
Crystallization and preliminary X-ray analysis of the complex of pig muscle D-glyceraldehyde-3-phosphate dehydrogenase with o-phenanthroline, 1994. ,
Profile analysis in single-crystal diffractometry, Acta Crystallographica Section A: Crystal Physics, Diffraction, Theoretical and General Crystallography, vol.25, issue.1, pp.43-55, 1969. ,
DOI : 10.1107/S0567739469000064
Principles of Protein X-ray Crystallography (Cantor, 1994. ,
Crystallization of Nucleic Acids and Proteins : A Practical Approach, 1992. ,
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
Structures of human and porcine aldehyde reductase: An enzyme implicated in diabetic complications, Acta Crystallog, vol.50, issue.1, pp.859-868, 1994. ,
Structure of porcine aldehyde reductase holoenzyme, Nature Structural Biology, vol.4, issue.8, pp.687-692, 1995. ,
DOI : 10.1016/0168-9002(94)90720-X
Accurate bond and angle parameters for X-ray protein structure refinement, Acta Crystallographica Section A Foundations of Crystallography, vol.47, issue.4, 1991. ,
DOI : 10.1107/S0108767391001071
Expression of the glyceraldehyde-3-phosphate dehydrogenase gene from the extremely thermophilic archaebacterium Methanothermusfervidus in E. coli. FEBS leU, pp.213-217, 1988. ,
An aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme, Biochemistry, vol.30, issue.26, pp.6397-6401, 1991. ,
DOI : 10.1021/bi00240a008
Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2??5 ?? resolution: Refinement of the atomic model, Journal of Molecular Biology, vol.97, issue.2, pp.237-256, 1975. ,
DOI : 10.1016/S0022-2836(75)80037-4
Subunit structure and activity of glyceraldehyde-3-phosphate dehydrogenase from spinach chloroplasts, Biochimica et Biophysica Acta (BBA) - Enzymology, vol.522, issue.1, pp.19-31, 1978. ,
DOI : 10.1016/0005-2744(78)90318-2
Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.1041, issue.1, pp.36-42, 1990. ,
DOI : 10.1016/0167-4838(90)90119-Z
Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Â resolution. II. Environment of bound NADPH and implications for catalysis, J. Biol. Chem, vol.257, pp.13663-13672, 1982. ,
The refined structure of beef liver catalase al 2.5 Â resolution. Acta Crystallog, pp.497-515, 1986. ,
Old yellow enzyme at 2 ?? resolution: overall structure, ligand binding, and comparison with related flavoproteins, Structure, vol.2, issue.11, pp.1089-1105, 1994. ,
DOI : 10.1016/S0969-2126(94)00111-1
Experiences with a new translation-function program, Journal of Applied Crystallography, vol.20, issue.6, pp.517-521, 1987. ,
DOI : 10.1107/S0021889887086102
The refined three-dimensional structure of 3??,20??-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases, Structure, vol.2, issue.7, pp.629-640, 1994. ,
DOI : 10.1016/S0969-2126(00)00064-2
Crystal Structure ofProteus mirabilisPR Catalase With and Without Bound NADPH, Journal of Molecular Biology, vol.249, issue.5, pp.933-954, 1995. ,
DOI : 10.1006/jmbi.1995.0350
Molecular symmetry of glyceraldehyde-3-phosphate dehydrogenase from Bacillus coagulans, Journal of Molecular Biology, vol.169, issue.4, pp.963-974, 1983. ,
DOI : 10.1016/S0022-2836(83)80145-4
Characterization and nucleotide binding properties of a mutant dihydropteridine reductase containing an aspartate 37-isoleucine replacement, J. Biol. Chem, vol.267, pp.15334-15339, 1992. ,
Importance of lysine-286 at the NADP site of glutamate dehydrogenase from Salmonella typhimurium, Biochemistry, vol.31, issue.34, pp.7807-7814, 1992. ,
DOI : 10.1021/bi00149a010
cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases, European Journal of Biochemistry, vol.14, issue.2, pp.479-484, 1989. ,
DOI : 10.1146/annurev.biophys.15.1.321
Helix stop signals in proteins and peptides: The capping box, Biochemistry, vol.32, issue.30, pp.7605-7609, 1993. ,
DOI : 10.1021/bi00081a001
Glyceraldehyde 3-phosphate dehydrogenases, Journal of Molecular Biology, vol.13, issue.3, pp.876-884, 1965. ,
DOI : 10.1016/S0022-2836(65)80151-6
Glyceraldehyde-3-phosphate dehydrogenase, The Enzymes, pp.1-49, 1976. ,
A point-focusing camera for single-crystal diffraction, Journal of Applied Crystallography, vol.1, issue.2, pp.84-90, 1968. ,
DOI : 10.1107/S0021889868005054
Crystal structure of NADH oxidase from Thermus thermophilus, Nature Structural & Molecular Biology, vol.47, issue.12, pp.1109-1114, 1995. ,
DOI : 10.1107/S0021889891004399
Stereochemically restrained refinement of macromolecular structures. Methods in Enzymol, pp.252-270, 1985. ,
The ??-helix dipole and the properties of proteins, Nature, vol.250, issue.5662, pp.443-446, 1978. ,
DOI : 10.1111/j.1432-1033.1972.tb01754.x
The role of the ??-helix dipole in protein function and structure, Progress in Biophysics and Molecular Biology, vol.45, issue.3, pp.149-195, 1985. ,
DOI : 10.1016/0079-6107(85)90001-X
Three-dimensional structure of rat liver 3a-hydroxysteroidldihydrodiol dehydrogenase: A member of the aldo-keto reductase superfamily, 1994. ,
Role of lysine-54 in determining cofactor specificity and binding in human dihydrofolate reductase, Biochemistry, vol.29, issue.35, pp.8063-8069, 1990. ,
DOI : 10.1021/bi00487a011
Catalytic mechanism of NADP+-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes, Biochemistry, vol.30, issue.35, pp.8671-8678, 1991. ,
DOI : 10.1021/bi00099a026
Structure of 3???isopropylmalate dehydrogenase in complex with NAD+: ligand???induced loop closing and mechanism for cofactor specificity, Structure, vol.2, issue.11, pp.1007-1017, 1994. ,
DOI : 10.1016/S0969-2126(94)00104-9
Sparse matrix sampling: a screening method for crystallization of proteins, Journal of Applied Crystallography, vol.24, issue.4, 1991. ,
DOI : 10.1107/S0021889891004430
Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector, Journal of Applied Crystallography, vol.21, issue.6, pp.916-924, 1988. ,
DOI : 10.1107/S0021889888007903
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
Refined structure of glutathione reductase at 1.54 ?? resolution, Journal of Molecular Biology, vol.195, issue.3, pp.701-729, 1987. ,
DOI : 10.1016/0022-2836(87)90191-4
Determinants of protein thermostability observed in the 1.9-.ANG. crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus, Biochemistry, vol.32, issue.15, pp.3913-3922, 1993. ,
DOI : 10.1021/bi00066a010
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
Cloning and sequencing of the putative glyceraldehyde-3-phosphate dehydrogenase gene from Cephalosporium acremonium and its application to heterologous gene expression, Journal of Fermentation and Bioengineering, vol.71, issue.3, pp.145-150 ,
DOI : 10.1016/0922-338X(91)90100-U
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
Moiscript: A program to produce both detailed and schematic plots of protein structures, J, 1991. ,
Structural comparisons lead to the definition of a new superfamily of NAD(P)(H)-accepting oxidoreductases: the single-domain reductases/epimerases/dehydrogenases (the ???RED??? family), Biochemical Journal, vol.304, issue.1, pp.95-99, 1994. ,
DOI : 10.1042/bj3040095
High Resolution Structures of Holo and Apo Formate Dehydrogenase, Journal of Molecular Biology, vol.236, issue.3, pp.759-785, 1994. ,
DOI : 10.1006/jmbi.1994.1188
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
Site-directed mutagenesis of a serine residue in cinnamyl alcohol dehydrogenase, a plant NADPH-dependent dehydrogenase, affects the specificity for the coenzyme, Biochemisfly, vol.34, pp.12426-12434, 1995. ,
Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 angstrom resolution, Science, vol.268, issue.5218, pp.1758-1762, 1995. ,
DOI : 10.1126/science.7792601
NAD-binding domains of dehydrogenases. Cu1' 1'. Opinion Struct, Biol, vol.5, pp.775-783, 1995. ,
Coenzyme binding in crystals of glyceraldehyde-3-phosphate dehydrogenase, Journal of Molecular Biology, vol.165, issue.2, pp.375-391, 1983. ,
DOI : 10.1016/S0022-2836(83)80262-9
Identification of an Arginine Residue in the Dual Coenzyme-Specific Glucose-6-Phosphate Dehydrogenase fromLeuconostoc mesenteroidesThat Plays a Key Role in Binding NADP+but Not NAD+, Archives of Biochemistry and Biophysics, vol.326, issue.1, pp.145-151, 1996. ,
DOI : 10.1006/abbi.1996.0058
Structure of D-Glyceraldehyde-3-Phosphate Dehydrogenase from Palinurus versicolor Carrying the Fluorescent NAD Derivatives at 2.7?? Resolution, Archives of Biochemistry and Biophysics, vol.302, issue.1, pp.161-166, 1993. ,
DOI : 10.1006/abbi.1993.1194
Traitement statistique des erreurs dans la determination des structures cristallines, Acta Crystallographica, vol.5, issue.6, pp.802-810, 1952. ,
DOI : 10.1107/S0365110X52002161
URL : http://journals.iucr.org/q/issues/1952/06/00/a00752/a00752.pdf
Prokaryotic features of a nucleus-encoded enzyme. cDNA sequences for chloroplast and cytosolic glyceraldehyde-3-phosphate dehydrogenases from mustard (Sinapis alba), European Journal of Biochemistry, vol.5, issue.2, pp.323-331, 1986. ,
DOI : 10.1016/S0076-6879(80)65059-9
Evidence for a chimeric nature of nuclear genomes: eubacterial origin of eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes., Proc. Nat/. Acad, 1993. ,
DOI : 10.1073/pnas.90.18.8692
New flavoenzymes, Current Opinion in Structural Biology, vol.1, issue.6, pp.954-967, 1991. ,
DOI : 10.1016/0959-440X(91)90091-7
The refined crystal structure ofPseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 ?? resolution, Proteins: Structure, Function, and Genetics, vol.352, issue.4, pp.336-351, 1992. ,
DOI : 10.1107/S0108767386099622
Dihydrofolate reductase from Lactobacil/us casei. X-ray structure of the enzyme-methotrexate-NADPH complex, J. Biol. Chem, vol.253, pp.6946-6954, 1978. ,
PracticaL Protein Clystal/ography, 1993. ,
Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin, Biochemistry, vol.31, issue.32, pp.7264-7273, 1992. ,
DOI : 10.1021/bi00147a009
Twinning in crystals of human skeletal muscle d-glyceraldehyde-3-phosphate dehydrogenase, Journal of Molecular Biology, vol.104, issue.1, pp.277-283, 1976. ,
DOI : 10.1016/0022-2836(76)90013-9
Amino Acid Substitutions in the Yeast Pichia Stipitis Xylitol Dehydrogenase Coenzyme-Binding Domain Affect the Coenzyme Specificity, European Journal of Biochemistry, vol.187, issue.1, pp.50-54, 1995. ,
DOI : 10.1038/343038a0
Anatomy of an engineered NAD-binding site, Protein Science, vol.187, issue.9, pp.1504-1514, 1994. ,
DOI : 10.1042/bj2450875
Structure of glutathione reductase from escherichia coli at 1.86 ?? resolution: Comparison with the enzyme from human erythrocytes, Protein Science, vol.250, issue.5, pp.799-809, 1994. ,
DOI : 10.1042/bj2450875
HB8, "Protein Engineering, Design and Selection", vol.7, issue.3, pp.401-403, 1994. ,
DOI : 10.1093/protein/7.3.401
Protein Recognition of Adenylate: An Example of a Fuzzy Recognition Template, Journal of Molecular Biology, vol.263, issue.3, pp.486-500, 1996. ,
DOI : 10.1006/jmbi.1996.0591
Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase, J. Bio/. Chem, vol.250, pp.9137-9162, 1975. ,
in the formation of charge-transfer transition in glyceraldehyde-3-phosphate dehydrogenase, "Protein Engineering, Design and Selection", vol.2, issue.1, pp.859-872, 1988. ,
DOI : 10.1093/protein/2.1.45
Structure of lobster apo-d-glyceraldehyde-3-phosphate dehydrogenase at 3.0 ?? resolution, Journal of Molecular Biology, vol.138, issue.4, pp.859-872, 1980. ,
DOI : 10.1016/0022-2836(80)90069-8
On the fast rotation function, Acta Crystallographica Section A Foundations of Crystallography, vol.43, issue.5, pp.645-653, 1987. ,
DOI : 10.1107/S0108767387098787
: an automated package for molecular replacement, Acta Crystallographica Section A Foundations of Crystallography, vol.50, issue.2, pp.157-163, 1994. ,
DOI : 10.1107/S0108767393007597
Crystal structure of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus at 2.2 Â resolution. An example of strong asymmetry between subunits, J. Mol, 1995. ,
Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis, J. Biol. Chem, vol.268, pp.4656-4660, 1993. ,
Crystallization and preliminary X-ray diffraction studies of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase, Acta Cryst, vol.51, pp.245-247, 1995. ,
Oscillation data reduction program, Proceedings of the CCP4 study weekend : data collection and processing, pp.56-62, 1993. ,
Variations on a theme: the family of FAD-dependent NAD(P)H-(disulphide)-oxidoreductases, Current Opinion in Structural Biology, vol.1, issue.5, 1991. ,
DOI : 10.1016/0959-440X(91)90181-R
Strong functional GC pressure in a light-regulated maize gene encoding subunit GAPA of chloroplast glyceraldehyde-3-phosphate dehydrogenase: Implications for the evolution of GAPA pseudogenes, Journal of Molecular Evolution, vol.23, issue.5, pp.412-421, 1989. ,
DOI : 10.1007/978-1-4684-4988-4_1
The mechanism of oxidation of aldehydes by glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chel1l, vol.198, issue.1, pp.731-743, 1952. ,
Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase, Structure, vol.3, issue.9, pp.927-938, 1995. ,
DOI : 10.1016/S0969-2126(01)00227-1
Etude des facteurs moléculaires responsables de la spécificité de cofacteur des. déshydrogénases à NAD(P), Thèse de l'Université H. Poincaré, 1994. ,
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
URL : https://doi.org/10.1016/s0006-3495(65)86759-5
Interaction of Pyridine Nucleodide Substrates with Escherichia coli Dihydrodipicolinate Reductase : Thermodynamic and Structural Analysis of Binary Complexes, Biochel1listry, vol.35, pp.13294-13302, 1996. ,
Cryocrystallography, Structure, vol.2, issue.12, pp.1135-1140, 1994. ,
DOI : 10.1016/S0969-2126(94)00116-2
Molecular symmetry axes and subunit interfaces in certain dehydrogenases, Journal of Molecular Biology, vol.76, issue.4, pp.533-537, 1973. ,
DOI : 10.1016/0022-2836(73)90491-9
Chemical and biological evolution of a nucleotide-binding protein, Nature, vol.243, issue.5463, pp.194-199, 1974. ,
DOI : 10.1101/SQB.1972.036.01.032
2 Evolutionary and Structural Relationships among Dehydrogenases, The Enzymes, pp.61-102, 1975. ,
DOI : 10.1016/S1874-6047(08)60210-3
TURBO-FRODO, Silicon Graphies Geometry Par1ner DirectOlY (SiliconGraphics, pp.77-78, 1989. ,
Loop and Subdomain Movements in the Mechanism of Escherichia Coli Dihydrofolate Reductase : Crystallographic Evidence, pp.586-603, 1997. ,
Three-Dimensional Structure of Escherichia coli Dihydrodipicolinate Reductase, Biochemistry, vol.34, issue.11, pp.3502-3512, 1995. ,
DOI : 10.1021/bi00011a003
The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase, Struct. Biol, vol.2, pp.69-76, 1995. ,
Binding of nucleotides by proteins, Current Opinion in Structural Biology, vol.2, issue.1, pp.61-67, 1992. ,
DOI : 10.1016/0959-440X(92)90178-A
Redesign of the coenzyme specificity of a dehydrogenase by protein
engineering, Nature, vol.343, issue.6253, pp.38-43, 1990. ,
DOI : 10.1038/343038a0
Sequence deterrninants of the capping box, a stabilizing motif at the N-termini-of a-helices, pp.1741-1745, 1994. ,
The raie of sulfhydryl groups in the activity of D-glyceraldehyde-3- phosphate dehydrogenase, J. Biol. Chem, vol.204, pp.265-281, 1953. ,
Interaction with arginine 597 of NADPH-cytochrome P-450 oxidoreductase is a primary source of the uniform binding energy used to discriminate between NADPH and NADH, Biochemistry, vol.32, issue.43, pp.11548-11558, 1993. ,
DOI : 10.1021/bi00094a011
Evidence in favor of the symbiotic origin of chloroplasts - Primary structure and evolution of tobacco glyceraldehyde-3-phosphate dehydragenases, Ce Il, vol.47, pp.73-80, 1986. ,
Crystal Structure ofEscherichia coliQOR Quinone Oxidoreductase Complexed with NADPH, Journal of Molecular Biology, vol.249, issue.4, pp.785-799, 1995. ,
DOI : 10.1006/jmbi.1995.0337
Crystal structure of rat liver dihydropteridine reductase., Proc. Natl. Acad. Sei. USA, pp.6080-6084, 1992. ,
DOI : 10.1073/pnas.89.13.6080
Refined 3.2 ?? structure of glycosomal holo glyceraldehyde phosphate dehydrogenase from Trypanosoma brucei brucei, Acta Crystallographica Section D Biological Crystallography, vol.51, issue.4, pp.575-589, 1995. ,
DOI : 10.1107/S0907444995003015
Crystal structure of Escherichia coli thioredoxin reductase refined at 2 Â resolution. Implications for a large conformational change during catalysis, 1994. ,
Structure of Glyceraldehyde-3-Phosphate Dehydrogenase: Structural Symmetry Within the Molecule, Nature, vol.197, issue.4962, pp.918-920, 1964. ,
DOI : 10.1021/ja01646a025
Low Resolution Structure of Glyceraldehyde 3-Phosphate Dehydrogenase, Nature New Biology, vol.240, issue.100, pp.130-139, 1972. ,
DOI : 10.1038/newbio240130a0
Interaction of pyrophosphate moieties with .alpha.-helixes in dinucleotide-binding proteins, Biochemistry, vol.24, issue.6, pp.1346-1357, 1985. ,
DOI : 10.1021/bi00327a012
Prediction of the occurrence of the ADP-binding ??????-fold in proteins, using an amino acid sequence fingerprint, Journal of Molecular Biology, vol.187, issue.1, pp.1-07, 1986. ,
DOI : 10.1016/0022-2836(86)90409-2
Refined 1.8 Â structure of lIUtlrdlll..,Sll\f;\~' reductase complexed with the potent inhibitor zopolrestat, Proc. Nat!. Acad. Sei. USA 90, pp.9847-98, 1993. ,
Crystallization and Crystal Data of Monellin, Proc. Natl. Acad. Sei. n, p.398, 1975. ,
DOI : 10.1073/pnas.72.1.398
Role of Arg231 and Tyr 284 of ThernlUs thermophilus isocitrate dehydrogenase in the coenzyme specificity, FEBS Let!, vol.355, pp.17-172, 1994. ,
[9] Stereospecificities of the pyridine nucleotide-linked enzymes, Methods in Enzymol, vol.87, issue.10, pp.1-126, 1982. ,
DOI : 10.1016/S0076-6879(82)87011-0