메뉴 건너뛰기




Volumn 357, Issue 5, 2006, Pages 1483-1499

1.6 Å crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: Novel fold topology revealed

Author keywords

Crystal structure; Pathogenic bacterium; Permutated fold; Secreted AroQ class chorismate mutase; Transition state analog complex

Indexed keywords

CHORISMATE MUTASE; DIMER; LIGAND; POLYPEPTIDE; BACTERIAL PROTEIN;

EID: 33645047892     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.01.069     Document Type: Article
Times cited : (54)

References (60)
  • 2
    • 0037621429 scopus 로고    scopus 로고
    • Charge optimization increases the potency and selectivity of a chorismate mutase inhibitor
    • A. Mandal, and D. Hilvert Charge optimization increases the potency and selectivity of a chorismate mutase inhibitor J. Am. Chem. Soc. 125 2003 5598 5599
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5598-5599
    • Mandal, A.1    Hilvert, D.2
  • 3
    • 0000682795 scopus 로고
    • The uncatalyzed Claisen rearrangement of chorismate to prephenate prefers a transition state of chairlike geometry
    • S.D. Copley, and J.R. Knowles The uncatalyzed Claisen rearrangement of chorismate to prephenate prefers a transition state of chairlike geometry J. Am. Chem. Soc. 107 1985 5306 5308
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 5306-5308
    • Copley, S.D.1    Knowles, J.R.2
  • 4
    • 33845377155 scopus 로고
    • An inhibitor of chorismate mutase resembling the transition-state conformation
    • P.A. Bartlett, and C.R. Johnson An inhibitor of chorismate mutase resembling the transition-state conformation J. Am. Chem. Soc. 107 1985 7792 7793
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 7792-7793
    • Bartlett, P.A.1    Johnson, C.R.2
  • 5
    • 0017747586 scopus 로고
    • Rearrangement of chorismate to prephenate. Use of chorismate mutase inhibitors to define the transition state structure
    • P.R. Andrews, E.N. Cain, E. Rizzardo, and G.D. Smith Rearrangement of chorismate to prephenate. Use of chorismate mutase inhibitors to define the transition state structure Biochemistry 16 1977 4848 4852
    • (1977) Biochemistry , vol.16 , pp. 4848-4852
    • Andrews, P.R.1    Cain, E.N.2    Rizzardo, E.3    Smith, G.D.4
  • 6
    • 0000267583 scopus 로고
    • Stereochemistry of the rearrangement of chorismate to prephenate: Chorismate mutase involves a chair transition state
    • S.G. Sogo, T.S. Widlanski, J.H. Hoare, C.E. Grimshaw, G.A. Berchtold, and J.R. Knowles Stereochemistry of the rearrangement of chorismate to prephenate: chorismate mutase involves a chair transition state J. Am. Chem. Soc. 106 1984 2701 2703
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 2701-2703
    • Sogo, S.G.1    Widlanski, T.S.2    Hoare, J.H.3    Grimshaw, C.E.4    Berchtold, G.A.5    Knowles, J.R.6
  • 7
    • 0033518886 scopus 로고    scopus 로고
    • Heavy atom isotope effects reveal a highly polarized transition state for chorismate mutase
    • D.J. Gustin, P. Mattei, P. Kast, O. Wiest, L. Lee, W.W. Cleland, and D. Hilvert Heavy atom isotope effects reveal a highly polarized transition state for chorismate mutase J. Am. Chem. Soc. 121 1999 1756 1757
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1756-1757
    • Gustin, D.J.1    Mattei, P.2    Kast, P.3    Wiest, O.4    Lee, L.5    Cleland, W.W.6    Hilvert, D.7
  • 9
    • 0021102421 scopus 로고
    • Secondary tritium isotope effects as probes of the enzymic and nonenzymic conversion of chorismate to prephenate
    • L. Addadi, E.K. Jaffe, and J.R. Knowles Secondary tritium isotope effects as probes of the enzymic and nonenzymic conversion of chorismate to prephenate Biochemistry 22 1983 4494 4501
    • (1983) Biochemistry , vol.22 , pp. 4494-4501
    • Addadi, L.1    Jaffe, E.K.2    Knowles, J.R.3
  • 11
    • 0015819741 scopus 로고
    • Transition-state stabilization and enzymic catalysis. Kinetic and molecular orbital studies of the rearrangement of chorismate to prephenate
    • P.R. Andrews, G.D. Smith, and I.G. Young Transition-state stabilization and enzymic catalysis. Kinetic and molecular orbital studies of the rearrangement of chorismate to prephenate Biochemistry 12 1973 3492 3498
    • (1973) Biochemistry , vol.12 , pp. 3492-3498
    • Andrews, P.R.1    Smith, G.D.2    Young, I.G.3
  • 12
    • 0038615889 scopus 로고    scopus 로고
    • Contributions of conformational compression and preferential transition state stabilization to the rate enhancement by chorismate mutase
    • C.R.W. Guimarães, M.P. Repasky, J. Chandrasekhar, J. Tirado-Rives, and W.L. Jorgensen Contributions of conformational compression and preferential transition state stabilization to the rate enhancement by chorismate mutase J. Am. Chem. Soc. 125 2003 6892 6899
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6892-6899
    • Guimarães, C.R.W.1    Repasky, M.P.2    Chandrasekhar, J.3    Tirado-Rives, J.4    Jorgensen, W.L.5
  • 13
    • 0041429611 scopus 로고    scopus 로고
    • Apparent NAC effect in chorismate mutase reflects electrostatic transition state stabilization
    • M. Štrajbl, A. Shurki, M. Kato, and A. Warshel Apparent NAC effect in chorismate mutase reflects electrostatic transition state stabilization J. Am. Chem. Soc. 125 2003 10228 10237
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10228-10237
    • Štrajbl, M.1    Shurki, A.2    Kato, M.3    Warshel, A.4
  • 14
    • 23244446189 scopus 로고    scopus 로고
    • A definitive mechanism for chorismate mutase
    • X. Zhang, X. Zhang, and T.C. Bruice A definitive mechanism for chorismate mutase Biochemistry 44 2005 10443 10448
    • (2005) Biochemistry , vol.44 , pp. 10443-10448
    • Zhang, X.1    Zhang, X.2    Bruice, T.C.3
  • 15
    • 0027274818 scopus 로고
    • Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog
    • Y.M. Chook, H. Ke, and W.N. Lipscomb Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog Proc. Natl Acad. Sci. USA 90 1993 8600 8603
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8600-8603
    • Chook, Y.M.1    Ke, H.2    Lipscomb, W.N.3
  • 16
    • 0027992458 scopus 로고
    • The monofunctional chorismate mutase from Bacillus subtilis: Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction
    • Y.M. Chook, J.V. Gray, H. Ke, and W.N. Lipscomb The monofunctional chorismate mutase from Bacillus subtilis: structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction J. Mol. Biol. 240 1994 476 500
    • (1994) J. Mol. Biol. , vol.240 , pp. 476-500
    • Chook, Y.M.1    Gray, J.V.2    Ke, H.3    Lipscomb, W.N.4
  • 18
    • 0029999832 scopus 로고    scopus 로고
    • Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: The importance of electrostatic catalysis
    • P. Kast, M. Asif-Ullah, N. Jiang, and D. Hilvert Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: the importance of electrostatic catalysis Proc. Natl Acad. Sci. USA 93 1996 5043 5048
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5043-5048
    • Kast, P.1    Asif-Ullah, M.2    Jiang, N.3    Hilvert, D.4
  • 19
    • 0034711227 scopus 로고    scopus 로고
    • A strategically positioned cation is crucial for efficient catalysis by chorismate mutase
    • P. Kast, C. Grisostomi, I.A. Chen, S. Li, U. Krengel, Y. Xue, and D. Hilvert A strategically positioned cation is crucial for efficient catalysis by chorismate mutase J. Biol. Chem. 275 2000 36832 36838
    • (2000) J. Biol. Chem. , vol.275 , pp. 36832-36838
    • Kast, P.1    Grisostomi, C.2    Chen, I.A.3    Li, S.4    Krengel, U.5    Xue, Y.6    Hilvert, D.7
  • 20
    • 0142052240 scopus 로고    scopus 로고
    • Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor
    • A. Kienhöfer, P. Kast, and D. Hilvert Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor J. Am. Chem. Soc. 125 2003 3206 3207
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3206-3207
    • Kienhöfer, A.1    Kast, P.2    Hilvert, D.3
  • 23
    • 0029278692 scopus 로고
    • New insight into the catalytic mechanism of chorismate mutases from structural studies
    • A.Y. Lee, J.D. Stewart, J. Clardy, and B. Ganem New insight into the catalytic mechanism of chorismate mutases from structural studies Chem. Biol. 2 1995 195 203
    • (1995) Chem. Biol. , vol.2 , pp. 195-203
    • Lee, A.Y.1    Stewart, J.D.2    Clardy, J.3    Ganem, B.4
  • 24
    • 0032516484 scopus 로고    scopus 로고
    • A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii
    • G. MacBeath, P. Kast, and D. Hilvert A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii Biochemistry 37 1998 10062 10073
    • (1998) Biochemistry , vol.37 , pp. 10062-10073
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 25
    • 0029109922 scopus 로고
    • Atomic structure of the buried catalytic pocket of Escherichia coli chorismate mutase
    • A.Y. Lee, P.A. Karplus, B. Ganem, and J. Clardy Atomic structure of the buried catalytic pocket of Escherichia coli chorismate mutase J. Am. Chem. Soc. 117 1995 3627 3628
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3627-3628
    • Lee, A.Y.1    Karplus, P.A.2    Ganem, B.3    Clardy, J.4
  • 27
    • 0031573452 scopus 로고    scopus 로고
    • Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures
    • N. Sträter, G. Schnappauf, G. Braus, and W.N. Lipscomb Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures Structure 5 1997 1437 1452
    • (1997) Structure , vol.5 , pp. 1437-1452
    • Sträter, N.1    Schnappauf, G.2    Braus, G.3    Lipscomb, W.N.4
  • 28
    • 0035235980 scopus 로고    scopus 로고
    • The emerging periplasm-localized subclass of AroQ chorismate mutases, exemplified by those from Salmonella typhimurium and Pseudomonas aeruginosa
    • D.H. Calhoun, C.A. Bonner, W. Gu, G. Xie, and R.A. Jensen The emerging periplasm-localized subclass of AroQ chorismate mutases, exemplified by those from Salmonella typhimurium and Pseudomonas aeruginosa Genome Biol. 2 2001 30.01 30.16
    • (2001) Genome Biol. , vol.2 , pp. 3001-3016
    • Calhoun, D.H.1    Bonner, C.A.2    Gu, W.3    Xie, G.4    Jensen, R.A.5
  • 29
    • 12544259906 scopus 로고    scopus 로고
    • Characterization of the secreted chorismate mutase from the pathogen Mycobacterium tuberculosis
    • S. Sasso, C. Ramakrishnan, M. Gamper, D. Hilvert, and P. Kast Characterization of the secreted chorismate mutase from the pathogen Mycobacterium tuberculosis FEBS J. 272 2005 375 389
    • (2005) FEBS J. , vol.272 , pp. 375-389
    • Sasso, S.1    Ramakrishnan, C.2    Gamper, M.3    Hilvert, D.4    Kast, P.5
  • 30
    • 0033118834 scopus 로고    scopus 로고
    • Cloning and characterization of an esophageal-gland-specific chorismate mutase from the phytoparasitic nematode Meloidogyne javanica
    • K.N. Lambert, K.D. Allen, and I.M. Sussex Cloning and characterization of an esophageal-gland-specific chorismate mutase from the phytoparasitic nematode Meloidogyne javanica Mol. Plant-Microbe Interact. 12 1999 328 336
    • (1999) Mol. Plant-Microbe Interact. , vol.12 , pp. 328-336
    • Lambert, K.N.1    Allen, K.D.2    Sussex, I.M.3
  • 31
    • 0034442207 scopus 로고    scopus 로고
    • DNA sequence and comparison of virulence plasmids from Rhodococcus equi ATCC 33701 and 103
    • S. Takai, S.A. Hines, T. Sekizaki, V.M. Nicholson, D.A. Alperin, and M. Osaki DNA sequence and comparison of virulence plasmids from Rhodococcus equi ATCC 33701 and 103 Infect. Immun. 68 2000 6840 6847
    • (2000) Infect. Immun. , vol.68 , pp. 6840-6847
    • Takai, S.1    Hines, S.A.2    Sekizaki, T.3    Nicholson, V.M.4    Alperin, D.A.5    Osaki, M.6
  • 32
    • 0036229497 scopus 로고    scopus 로고
    • Examination of Salmonella gene expression in an infected mammalian host using the green fluorescent protein and two-colour flow cytometry
    • D. Bumann Examination of Salmonella gene expression in an infected mammalian host using the green fluorescent protein and two-colour flow cytometry Mol. Microbiol. 43 2002 1269 1283
    • (2002) Mol. Microbiol. , vol.43 , pp. 1269-1283
    • Bumann, D.1
  • 33
    • 0037230588 scopus 로고    scopus 로고
    • Characterization of a chorismate mutase from the potato cyst nematode Globodera pallida
    • J.T. Jones, C. Furlanetto, E. Bakker, B. Banks, V. Blok, and Q. Chen Characterization of a chorismate mutase from the potato cyst nematode Globodera pallida Mol. Plant Pathol. 4 2003 43 50
    • (2003) Mol. Plant Pathol. , vol.4 , pp. 43-50
    • Jones, J.T.1    Furlanetto, C.2    Bakker, E.3    Banks, B.4    Blok, V.5    Chen, Q.6
  • 34
    • 0037406836 scopus 로고    scopus 로고
    • A chorismate mutase from the soybean cyst nematode Heterodera glycines shows polymorphisms that correlate with virulence
    • S. Bekal, T.L. Niblack, and K.N. Lambert A chorismate mutase from the soybean cyst nematode Heterodera glycines shows polymorphisms that correlate with virulence Mol. Plant-Microbe Interact. 16 2003 439 446
    • (2003) Mol. Plant-Microbe Interact. , vol.16 , pp. 439-446
    • Bekal, S.1    Niblack, T.L.2    Lambert, K.N.3
  • 35
    • 0037305598 scopus 로고    scopus 로고
    • Meloidogyne javanica chorismate mutase 1 alters plant cell development
    • E.A. Doyle, and K.N. Lambert Meloidogyne javanica chorismate mutase 1 alters plant cell development Mol. Plant-Microbe Interact. 16 2003 123 131
    • (2003) Mol. Plant-Microbe Interact. , vol.16 , pp. 123-131
    • Doyle, E.A.1    Lambert, K.N.2
  • 37
    • 21244483507 scopus 로고    scopus 로고
    • Purified recombinant hypothetical protein coded by open reading frame Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class of periplasmic chorismate mutase activity
    • P. Prakash, B. Aruna, A.A. Sardesai, and S.E. Hasnain Purified recombinant hypothetical protein coded by open reading frame Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class of periplasmic chorismate mutase activity J. Biol. Chem. 280 2005 19641 19648
    • (2005) J. Biol. Chem. , vol.280 , pp. 19641-19648
    • Prakash, P.1    Aruna, B.2    Sardesai, A.A.3    Hasnain, S.E.4
  • 38
    • 0031301406 scopus 로고    scopus 로고
    • The AroQ and PheA domains of the bifunctional P-protein from Xanthomonas campestris in a context of genomic comparison
    • W. Gu, D.S. Williams, H.C. Aldrich, G. Xie, D.W. Gabriel, and R.A. Jensen The AroQ and PheA domains of the bifunctional P-protein from Xanthomonas campestris in a context of genomic comparison Microb. Comp. Genomics 2 1997 141 158
    • (1997) Microb. Comp. Genomics , vol.2 , pp. 141-158
    • Gu, W.1    Williams, D.S.2    Aldrich, H.C.3    Xie, G.4    Gabriel, D.W.5    Jensen, R.A.6
  • 39
    • 2342642643 scopus 로고    scopus 로고
    • Directed evolution of protein enzymes using nonhomologous random recombination
    • J.A. Bittker, B.V. Le, J.M. Liu, and D.R. Liu Directed evolution of protein enzymes using nonhomologous random recombination Proc. Natl Acad. Sci. USA 101 2004 7011 7016
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7011-7016
    • Bittker, J.A.1    Le, B.V.2    Liu, J.M.3    Liu, D.R.4
  • 40
    • 0032549781 scopus 로고    scopus 로고
    • Redesigning enzyme topology by directed evolution
    • G. MacBeath, P. Kast, and D. Hilvert Redesigning enzyme topology by directed evolution Science 279 1998 1958 1961
    • (1998) Science , vol.279 , pp. 1958-1961
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 41
    • 0032456057 scopus 로고    scopus 로고
    • Probing enzyme quaternary structure by combinatorial mutagenesis and selection
    • G. MacBeath, P. Kast, and D. Hilvert Probing enzyme quaternary structure by combinatorial mutagenesis and selection Protein Sci. 7 1998 1757 1767
    • (1998) Protein Sci. , vol.7 , pp. 1757-1767
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 42
    • 0032479149 scopus 로고    scopus 로고
    • Tyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutase
    • G. Schnappauf, S. Krappmann, and G.H. Braus Tyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutase J. Biol. Chem. 273 1998 17012 17017
    • (1998) J. Biol. Chem. , vol.273 , pp. 17012-17017
    • Schnappauf, G.1    Krappmann, S.2    Braus, G.H.3
  • 43
    • 18744394070 scopus 로고    scopus 로고
    • Q-SiteFinder: An energy-based method for the prediction of protein-ligand binding sites
    • A.T.R. Laurie, and R.M. Jackson Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites Bioinformatics 21 2005 1908 1916
    • (2005) Bioinformatics , vol.21 , pp. 1908-1916
    • Laurie, A.T.R.1    Jackson, R.M.2
  • 45
    • 0029897906 scopus 로고    scopus 로고
    • Analysis of active site residues in Escherichia coli chorismate mutase by site-directed mutagenesis
    • D.R. Liu, S.T. Cload, R.M. Pastor, and P.G. Schultz Analysis of active site residues in Escherichia coli chorismate mutase by site-directed mutagenesis J. Am. Chem. Soc. 118 1996 1789 1790
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1789-1790
    • Liu, D.R.1    Cload, S.T.2    Pastor, R.M.3    Schultz, P.G.4
  • 46
    • 0030182905 scopus 로고    scopus 로고
    • Site-directed mutagenesis of monofunctional chorismate mutase engineered from the E. coli P-protein
    • S. Zhang, P. Kongsaeree, J. Clardy, D.B. Wilson, and B. Ganem Site-directed mutagenesis of monofunctional chorismate mutase engineered from the E. coli P-protein Bioorg. Med. Chem. 4 1996 1015 1020
    • (1996) Bioorg. Med. Chem. , vol.4 , pp. 1015-1020
    • Zhang, S.1    Kongsaeree, P.2    Clardy, J.3    Wilson, D.B.4    Ganem, B.5
  • 47
    • 25444445359 scopus 로고    scopus 로고
    • Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from combinatorial mutagenesis and selection
    • D.E. Künzler, S. Sasso, M. Gamper, D. Hilvert, and P. Kast Mechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from combinatorial mutagenesis and selection J. Biol. Chem. 280 2005 32827 32834
    • (2005) J. Biol. Chem. , vol.280 , pp. 32827-32834
    • Künzler, D.E.1    Sasso, S.2    Gamper, M.3    Hilvert, D.4    Kast, P.5
  • 48
    • 0030831256 scopus 로고    scopus 로고
    • A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditions
    • G. Schnappauf, N. Sträter, W.N. Lipscomb, and G.H. Braus A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditions Proc. Natl Acad. Sci. USA 94 1997 8491 8496
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 8491-8496
    • Schnappauf, G.1    Sträter, N.2    Lipscomb, W.N.3    Braus, G.H.4
  • 52
    • 0028103275 scopus 로고
    • The CCP4 Suite - Programs for protein crystallography
    • S. Bailey The CCP4 Suite - programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 54
    • 0022325950 scopus 로고
    • Resolution of phase ambiguity in macromolecular crystallography
    • B.C. Wang Resolution of phase ambiguity in macromolecular crystallography Methods Enzymol. 115 1985 90 112
    • (1985) Methods Enzymol. , vol.115 , pp. 90-112
    • Wang, B.C.1
  • 55
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nature Struct. Biol. 6 1999 458 463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 58
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • G.J. Kleywegt Use of non-crystallographic symmetry in protein structure refinement Acta Crystallog. sect. D 52 1996 842 857
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 842-857
    • Kleywegt, G.J.1
  • 59
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander 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
  • 60
    • 0000243829 scopus 로고
    • PROCHECK - A program to check the stereochemical quality of protein structures
    • R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.