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Volumn 285, Issue 4, 1999, Pages 1633-1653

A detailed structural description of Escherichia coli succinyl-CoA synthetase

Author keywords

Coenzyme A; Oligomer; Phosphorylated histidine; Succinyl CoA synthetase; X ray crystallography

Indexed keywords

COENZYME A; DIMER; HISTIDINE; NUCLEOTIDE BINDING PROTEIN; SUCCINYL COENZYME A SYNTHETASE; TETRAMER; THIOL GROUP;

EID: 0033614003     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2324     Document Type: Article
Times cited : (86)

References (56)
  • 2
    • 0001835759 scopus 로고
    • 3D search and research using the Cambridge structural database
    • Allen F. H., Kennard O. 3D search and research using the Cambridge structural database. Chem. Des. Automat. News. 8:1993;1-37.
    • (1993) Chem. Des. Automat. News , vol.8 , pp. 1-37
    • Allen, F.H.1    Kennard, O.2
  • 3
    • 0027179135 scopus 로고
    • Cloning, characterization, and expression of the β subunit of pig heart succinyl-CoA synthetase
    • Bailey D. L., Wolodko W. T., Bridger W. A. Cloning, characterization, and expression of the β subunit of pig heart succinyl-CoA synthetase. Protein Sci. 2:1993;1255-1262.
    • (1993) Protein Sci. , vol.2 , pp. 1255-1262
    • Bailey, D.L.1    Wolodko, W.T.2    Bridger, W.A.3
  • 4
    • 0033614008 scopus 로고    scopus 로고
    • A dimeric form of Escherichia coli succinyl-CoA synthetase produced by site-directed mutagenesis
    • Bailey D. L., Fraser M. E., Bridger W. A., James M. N. G., Wolodko W. T. A dimeric form of Escherichia coli succinyl-CoA synthetase produced by site-directed mutagenesis. J. Mol. Biol. 285:1998;1655-1666.
    • (1998) J. Mol. Biol. , vol.285 , pp. 1655-1666
    • Bailey, D.L.1    Fraser, M.E.2    Bridger, W.A.3    James, M.N.G.4    Wolodko, W.T.5
  • 5
    • 0014419170 scopus 로고
    • The crystal structure of 1,3-diphosphorylimidazole
    • Beard L. N., Lenhert P. G. The crystal structure of 1,3-diphosphorylimidazole. Acta Crystallog. sect. B. 24:1968;1529-1539.
    • (1968) Acta Crystallog. Sect. B , vol.24 , pp. 1529-1539
    • Beard, L.N.1    Lenhert, P.G.2
  • 8
    • 0024318378 scopus 로고
    • Overexpression and site-directed mutagenesis of the succinyl-CoA synthetase of Escherichia coli and nucleotide sequence of a gene (g30) that is adjacent to the suc operon
    • Buck D., Guest J. R. Overexpression and site-directed mutagenesis of the succinyl-CoA synthetase of Escherichia coli and nucleotide sequence of a gene (g30) that is adjacent to the suc operon. Biochem. J. 260:1989;737-747.
    • (1989) Biochem. J. , vol.260 , pp. 737-747
    • Buck, D.1    Guest, J.R.2
  • 10
    • 0017881630 scopus 로고
    • Affinity labeling of succinyl-CoA synthetase from porcine heart and Escherichia coli with oxidized coenzyme a disulfide
    • Collier G. E., Nishimura J. S. Affinity labeling of succinyl-CoA synthetase from porcine heart and Escherichia coli with oxidized coenzyme a disulfide. J. Biol. Chem. 253:1977;4938-4943.
    • (1977) J. Biol. Chem. , vol.253 , pp. 4938-4943
    • Collier, G.E.1    Nishimura, J.S.2
  • 11
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly M. L. Solvent-accessible surfaces of proteins and nucleic acids. Science. 221:1983;709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 12
    • 0030444352 scopus 로고    scopus 로고
    • The diverse world of coenzyme A binding proteins
    • Engel C., Wierenga R. The diverse world of coenzyme A binding proteins. Curr. Opin. Struct. Biol. 6:1996;790-797.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 790-797
    • Engel, C.1    Wierenga, R.2
  • 13
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R. A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 15
    • 0028151598 scopus 로고
    • Vancomycin resistance: Structure of D -alanine: D -alanine ligase at 2.3 Å resolution
    • Fan C., Moews P. C., Walsh C. T., Knox J. R. Vancomycin resistance: structure of D -alanine: D -alanine ligase at 2.3 Å resolution. Science. 266:1994;439-443.
    • (1994) Science , vol.266 , pp. 439-443
    • Fan, C.1    Moews, P.C.2    Walsh, C.T.3    Knox, J.R.4
  • 16
    • 0028860295 scopus 로고
    • A common fold for peptide synthetases cleaving ATP to ADP: Glutathione synthetase and D -alanine: D -alanine ligase of Escherichia coli
    • Fan C., Moews P. C., Shi Y., Walsh C. T., Knox J. R. A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D -alanine: D -alanine ligase of Escherichia coli. Proc. Natl Acad. Sci. USA. 92:1995;1172-1176.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1172-1176
    • Fan, C.1    Moews, P.C.2    Shi, Y.3    Walsh, C.T.4    Knox, J.R.5
  • 17
    • 0031467818 scopus 로고    scopus 로고
    • A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity
    • Galperin M. Y., Koonin E. V. A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci. 6:1997;2639-2643.
    • (1997) Protein Sci. , vol.6 , pp. 2639-2643
    • Galperin, M.Y.1    Koonin, E.V.2
  • 18
    • 0030598361 scopus 로고    scopus 로고
    • Disallowed Ramachandran conformations of amino acid residues in protein structures
    • Gunasekaran K., Ramakrishnan C., Balaram P. Disallowed Ramachandran conformations of amino acid residues in protein structures. J. Mol. Biol. 264:1996;191-198.
    • (1996) J. Mol. Biol. , vol.264 , pp. 191-198
    • Gunasekaran, K.1    Ramakrishnan, C.2    Balaram, P.3
  • 19
    • 0038228666 scopus 로고    scopus 로고
    • X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes
    • Hakansson K., Doherty A. J., Shuman S., Wigley D. B. X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell. 89:1997;545-553.
    • (1997) Cell , vol.89 , pp. 545-553
    • Hakansson, K.1    Doherty, A.J.2    Shuman, S.3    Wigley, D.B.4
  • 20
    • 0032539677 scopus 로고    scopus 로고
    • Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping
    • Hakansson K., Wigley D. B. Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping. Proc. Natl Acad. Sci. USA. 95:1998;1505-1510.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1505-1510
    • Hakansson, K.1    Wigley, D.B.2
  • 22
    • 0030021264 scopus 로고    scopus 로고
    • Structure of the multifunctional loops in the nonclassical ATP-binding fold of glutathione synthetase
    • Hibi T., Nishioka T., Kato H., Tanizawa K., Fukui T., Katsube Y., Oda J. Structure of the multifunctional loops in the nonclassical ATP-binding fold of glutathione synthetase. Nature Struct. Biol. 3:1996;16-18.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 16-18
    • Hibi, T.1    Nishioka, T.2    Kato, H.3    Tanizawa, K.4    Fukui, T.5    Katsube, Y.6    Oda, J.7
  • 23
    • 0002193613 scopus 로고
    • The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography
    • Higashi T. The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography. J. Appl. Crystallog. 22:1989;9-18.
    • (1989) J. Appl. Crystallog. , vol.22 , pp. 9-18
    • Higashi, T.1
  • 24
    • 0014959139 scopus 로고
    • The absolute configuration of pantothenic acid
    • Hill R. K., Chan T. H. The absolute configuration of pantothenic acid. Biochem. Biophys. Res. Commun. 38:1970;181-183.
    • (1970) Biochem. Biophys. Res. Commun. , vol.38 , pp. 181-183
    • Hill, R.K.1    Chan, T.H.2
  • 25
    • 0013872353 scopus 로고
    • The preparation and characterization of 1-phosphohistidine and 3-phosphohistidine
    • Hultquist D. E., Moyer R. W., Boyer P. D. The preparation and characterization of 1-phosphohistidine and 3-phosphohistidine. Biochemistry. 5:1966;322-331.
    • (1966) Biochemistry , vol.5 , pp. 322-331
    • Hultquist, D.E.1    Moyer, R.W.2    Boyer, P.D.3
  • 26
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF- A program to identify and analyze structural motifs in proteins
    • Hutchinson E. G., Thornton J. M. PROMOTIF- a program to identify and analyze structural motifs in proteins. Protein Sci. 5:1996;212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 27
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones T. A. Interactive computer graphics: FRODO. Methods Enzymol. 115:1985;157-171.
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 34
    • 0029900511 scopus 로고    scopus 로고
    • Determination of the nucleotide binding site within Clostridium symbiosum pyruvate phosphate dikinase by photoaffinity labeling, site-directed mutagenesis, and structural analysis
    • McGuire M., Carroll L. J., Yankie L., Thrall S. H., Dunaway-Mariano D., Herzberg O., Jayaram B., Haley B. H. Determination of the nucleotide binding site within Clostridium symbiosum pyruvate phosphate dikinase by photoaffinity labeling, site-directed mutagenesis, and structural analysis. Biochemistry. 35:1996;8544-8552.
    • (1996) Biochemistry , vol.35 , pp. 8544-8552
    • McGuire, M.1    Carroll, L.J.2    Yankie, L.3    Thrall, S.H.4    Dunaway-Mariano, D.5    Herzberg, O.6    Jayaram, B.7    Haley, B.H.8
  • 35
    • 0015524252 scopus 로고
    • Succinyl coenzyme A synthetase of Escherichia coli. Effects of phosphoenzyme formation and of substrate binding on the reactivity and stability of the enzyme
    • Moffet F. J., Wang T., Bridger W. A. Succinyl coenzyme A synthetase of Escherichia coli. Effects of phosphoenzyme formation and of substrate binding on the reactivity and stability of the enzyme. J. Biol. Chem. 247:1972;8139-8144.
    • (1972) J. Biol. Chem. , vol.247 , pp. 8139-8144
    • Moffet, F.J.1    Wang, T.2    Bridger, W.A.3
  • 36
    • 0029154302 scopus 로고
    • Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium
    • Morera S., Chiadmi M., LeBras G., Lascu I., Janin J. Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium. Biochemistry. 34:1995;11062-11070.
    • (1995) Biochemistry , vol.34 , pp. 11062-11070
    • Morera, S.1    Chiadmi, M.2    Lebras, G.3    Lascu, I.4    Janin, J.5
  • 37
    • 0029950031 scopus 로고    scopus 로고
    • Structural classification of proteins: New superfamilies
    • Murzin A. G. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 6:1996;386-394.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 386-394
    • Murzin, A.G.1
  • 38
    • 0028961335 scopus 로고
    • Scop: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin A. G., Brenner S. E., Hubbard T., Chothia C. scop: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:1995;536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 39
    • 0001146990 scopus 로고
    • Stereospecificity of creatine kinase. Crystal structure of 1-carboxymethyl-2-imino-3-phosphonoimidazolidine
    • Phillips G. N. Jr, Thomas J. W. Jr, Annesley T. M., Quiocho F. A. Stereospecificity of creatine kinase. Crystal structure of 1-carboxymethyl-2-imino-3-phosphonoimidazolidine. J. Am. Chem. Soc. 101:1979;7120-7121.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 7120-7121
    • Phillips G.N., Jr.1    Thomas J.W., Jr.2    Annesley, T.M.3    Quiocho, F.A.4
  • 40
    • 0028589065 scopus 로고
    • Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli
    • Rajagopal P., Waygood E. B., Klevit R. E. Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli. Biochemistry. 33:1994;15271-15282.
    • (1994) Biochemistry , vol.33 , pp. 15271-15282
    • Rajagopal, P.1    Waygood, E.B.2    Klevit, R.E.3
  • 41
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read R. J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A. 42:1986;140-149.
    • (1986) Acta Crystallog. Sect. a , vol.42 , pp. 140-149
    • Read, R.J.1
  • 42
    • 0030824253 scopus 로고    scopus 로고
    • Mutually exclusive splicing generates two distinct isoforms of pig heart succinyl-CoA synthetase
    • Ryan D. G., Lin T., Brownie E., Bridger W. A., Wolodko W. T. Mutually exclusive splicing generates two distinct isoforms of pig heart succinyl-CoA synthetase. J. Biol. Chem. 272:1997;21151-21159.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21151-21159
    • Ryan, D.G.1    Lin, T.2    Brownie, E.3    Bridger, W.A.4    Wolodko, W.T.5
  • 43
    • 0000293676 scopus 로고
    • X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation
    • Sakabe N. X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instrum. Methods Phys. Res. Sect. A. 303:1991;448-463.
    • (1991) Nucl. Instrum. Methods Phys. Res. Sect. a , vol.303 , pp. 448-463
    • Sakabe, N.1
  • 44
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7
    • Subramanya H. S., Doherty A. J., Ashford S. R., Wigley D. B. Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell. 85:1996;607-615.
    • (1996) Cell , vol.85 , pp. 607-615
    • Subramanya, H.S.1    Doherty, A.J.2    Ashford, S.R.3    Wigley, D.B.4
  • 45
    • 0000712703 scopus 로고
    • International Union of Crystallography world list of crystallographic computer programs
    • Thiessen W. E., Levy H. A. International Union of Crystallography world list of crystallographic computer programs. J. Appl. Crystallog. 6:1973;309.
    • (1973) J. Appl. Crystallog. , vol.6 , pp. 309
    • Thiessen, W.E.1    Levy, H.A.2
  • 46
    • 0030957783 scopus 로고    scopus 로고
    • Structure of carbamoyl phosphate synthetase: A journey of 96 Å from substrate to product
    • Thoden J. B., Holden H. M., Wesenberg G., Raushel F. M., Rayment I. Structure of carbamoyl phosphate synthetase: A journey of 96 Å from substrate to product. Biochemistry. 36:1997;6305-6316.
    • (1997) Biochemistry , vol.36 , pp. 6305-6316
    • Thoden, J.B.1    Holden, H.M.2    Wesenberg, G.3    Raushel, F.M.4    Rayment, I.5
  • 48
    • 84945074880 scopus 로고
    • Conjugate-direction minimization. An improved method for the refinement of macromolecules
    • Tronrud D. E. Conjugate-direction minimization. An improved method for the refinement of macromolecules. Acta Crystallog. sect. A. 48:1992;912-916.
    • (1992) Acta Crystallog. Sect. a , vol.48 , pp. 912-916
    • Tronrud, D.E.1
  • 49
    • 0028905499 scopus 로고
    • High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data
    • van Nuland N. A. J., Boelens R., Scheek R. M., Robillard G. T. High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data. J. Mol. Biol. 246:1995;180-193.
    • (1995) J. Mol. Biol. , vol.246 , pp. 180-193
    • Van Nuland, N.A.J.1    Boelens, R.2    Scheek, R.M.3    Robillard, G.T.4
  • 50
    • 0020484825 scopus 로고
    • Frequency-dependent phosphorus-31 nuclear magnetic resonance studies of the phosphohistidine residue of succinyl-CoA synthetase and the phosphoserine residue of glycogen phosphorylase a
    • Vogel H. J., Bridger W. A., Sykes B. D. Frequency-dependent phosphorus-31 nuclear magnetic resonance studies of the phosphohistidine residue of succinyl-CoA synthetase and the phosphoserine residue of glycogen phosphorylase a. Biochemistry. 21:1982;1126-1132.
    • (1982) Biochemistry , vol.21 , pp. 1126-1132
    • Vogel, H.J.1    Bridger, W.A.2    Sykes, B.D.3
  • 51
    • 0028085434 scopus 로고
    • Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase
    • Waldrop G. L., Rayment I., Holden H. M. Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry. 33:1994;10249-10256.
    • (1994) Biochemistry , vol.33 , pp. 10249-10256
    • Waldrop, G.L.1    Rayment, I.2    Holden, H.M.3
  • 52
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga R. K., Terpstra P., Hol W. G. J. Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187:1986;101-107.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 53
    • 0021356895 scopus 로고
    • Crystallization of succinyl-CoA synthetase from Escherichia coli
    • Wolodko W. T., James M. N. G., Bridger W. A. Crystallization of succinyl-CoA synthetase from Escherichia coli. J. Biol. Chem. 259:1984;5316-5320.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5316-5320
    • Wolodko, W.T.1    James, M.N.G.2    Bridger, W.A.3
  • 54
    • 0023055735 scopus 로고
    • Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli
    • Wolodko W. T., Kay C. M., Bridger W. A. Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli. Biochemistry. 25:1986;5420-5425.
    • (1986) Biochemistry , vol.25 , pp. 5420-5425
    • Wolodko, W.T.1    Kay, C.M.2    Bridger, W.A.3
  • 55
    • 0028276977 scopus 로고
    • The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-Å resolution
    • Wolodko W. T., Fraser M. E., James M. N. G., Bridger W. A. The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-Å resolution. J. Biol. Chem. 269:1994;10883-10890.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10883-10890
    • Wolodko, W.T.1    Fraser, M.E.2    James, M.N.G.3    Bridger, W.A.4
  • 56
    • 0027530140 scopus 로고
    • Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution
    • Yamaguchi H., Kato H., Hata Y., Nishioka T., Kimura A., Oda J., Katsube Y. Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution. J. Mol. Biol. 229:1993;1083-1100.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1083-1100
    • Yamaguchi, H.1    Kato, H.2    Hata, Y.3    Nishioka, T.4    Kimura, A.5    Oda, J.6    Katsube, Y.7


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