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Volumn 12, Issue 9, 2003, Pages 1822-1832

Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme a abortive ternary complex at 1.95 Å resolution

Author keywords

Citrate synthase; Cysteinesulfenic acid; Hydrogen abstraction; Malate synthase; Protein crystallography

Indexed keywords

ACETYL COENZYME A; ANTIINFECTIVE AGENT; ARGININE; ASPARTIC ACID; CITRATE SYNTHASE; COENZYME A; CYSTEINE; GLYOXYLIC ACID; HYDROGEN; ISOENZYME; MAGNESIUM; MALATE SYNTHASE; MALIC ACID; PYRUVIC ACID; SULFENIC ACID DERIVATIVE;

EID: 0041510314     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03174303     Document Type: Article
Times cited : (67)

References (61)
  • 1
    • 0028240897 scopus 로고
    • A new generation of information retrieval tools for biologists: The example of the ExPASy WWW server
    • Appel, R.D., Baroch, A., and Hochstrasser, D.F. 1994. A new generation of information retrieval tools for biologists: The example of the ExPASy WWW server. Trends. Biochem. Sci. 19: 258-261.
    • (1994) Trends. Biochem. Sci. , vol.19 , pp. 258-261
    • Appel, R.D.1    Baroch, A.2    Hochstrasser, D.F.3
  • 2
    • 0028104956 scopus 로고
    • Ligand binding onto maize (Zea mays) malate synthase: A structural study
    • Beeckmans, S., Khan, A.S., Kanarek, L., and van Driessche, E. 1994. Ligand binding onto maize (Zea mays) malate synthase: A structural study. Biochem. J. 303: 413-421.
    • (1994) Biochem. J. , vol.303 , pp. 413-421
    • Beeckmans, S.1    Khan, A.S.2    Kanarek, L.3    Van Driessche, E.4
  • 3
    • 12444290191 scopus 로고
    • Studies of the mechanism of action of the condensing enzyme
    • Bove, J., Martin, R.O., Ingraham, L.L., and Stumpf, P.K. 1959. Studies of the mechanism of action of the condensing enzyme. J. Biol. Chem. 234: 999-1003.
    • (1959) J. Biol. Chem. , vol.234 , pp. 999-1003
    • Bove, J.1    Martin, R.O.2    Ingraham, L.L.3    Stumpf, P.K.4
  • 5
  • 6
    • 0030893657 scopus 로고    scopus 로고
    • NADP-dependent enzymes, I: Conserved stereochemistry of cofactor binding
    • Carugo, O. and Argos, P. 1997. NADP-dependent enzymes, I: Conserved stereochemistry of cofactor binding. Proteins 28: 10-28.
    • (1997) Proteins , vol.28 , pp. 10-28
    • Carugo, O.1    Argos, P.2
  • 7
    • 0001110143 scopus 로고
    • Enols and other reactive species
    • Chiang, Y. and Kresge, A.J. 1991. Enols and other reactive species. Science 253: 395-400.
    • (1991) Science , vol.253 , pp. 395-400
    • Chiang, Y.1    Kresge, A.J.2
  • 8
    • 0009082529 scopus 로고
    • Comparative biochemistry of the glyoxylate cycle
    • Cioni, M., Pinzauti, G., and Vanni, P. 1981. Comparative biochemistry of the glyoxylate cycle. Comp. Biochem. Physiol. 70B: 1-26.
    • (1981) Comp. Biochem. Physiol. , vol.70 B , pp. 1-26
    • Cioni, M.1    Pinzauti, G.2    Vanni, P.3
  • 9
    • 0033598677 scopus 로고    scopus 로고
    • Protein-sulfenic acids: Diverse roles for an unlikely player in enzyme catalysis and redox regulation
    • Claiborne, A., Yeh, J.I., Mallett, T.C., Luba, J., Crane Jr., E., Charrier, V., and Parsonage, D. 1999. Protein-sulfenic acids: Diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38: 15407-15416.
    • (1999) Biochemistry , vol.38 , pp. 15407-15416
    • Claiborne, A.1    Yeh, J.I.2    Mallett, T.C.3    Luba, J.4    Crane E., Jr.5    Charrier, V.6    Parsonage, D.7
  • 10
    • 0023727337 scopus 로고
    • Malate synthase: Proof of a stepwise Claisen condensation using the double-isotope fractionation test
    • Clark, J.D., O'Keefe, S.J., and Knowles, J.R. 1988. Malate synthase: Proof of a stepwise Claisen condensation using the double-isotope fractionation test. Biochemistry 27: 5961-5971.
    • (1988) Biochemistry , vol.27 , pp. 5961-5971
    • Clark, J.D.1    O'Keefe, S.J.2    Knowles, J.R.3
  • 11
    • 0014694509 scopus 로고
    • Asymmetric methyl groups, and the mechanism of malate synthase
    • Cornforth, J.W., Redmond, J.W., Eggerer, H., Buckel, W., and Gutschow, C. 1969. Asymmetric methyl groups, and the mechanism of malate synthase. Nature 221: 1212-1213.
    • (1969) Nature , vol.221 , pp. 1212-1213
    • Cornforth, J.W.1    Redmond, J.W.2    Eggerer, H.3    Buckel, W.4    Gutschow, C.5
  • 13
    • 0035882572 scopus 로고    scopus 로고
    • Adenine recognition: A motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins
    • Denessiouk, K.A., Rantanen, V.V., and Johnson, M.S. 2001. Adenine recognition: A motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins. Proteins 44: 282-291.
    • (2001) Proteins , vol.44 , pp. 282-291
    • Denessiouk, K.A.1    Rantanen, V.V.2    Johnson, M.S.3
  • 14
  • 15
    • 0023715740 scopus 로고
    • Primary and post-irradiation inactivation of the sulfhydryl enzyme malate synthase: Correlation of protective effects of additives
    • Durchschlag, H. and Zipper, P. 1988. Primary and post-irradiation inactivation of the sulfhydryl enzyme malate synthase: Correlation of protective effects of additives. FEBS Lett. 237: 208-212.
    • (1988) FEBS Lett. , vol.237 , pp. 208-212
    • Durchschlag, H.1    Zipper, P.2
  • 16
    • 0019430726 scopus 로고
    • Large-scale purification and some properties of malate synthase from baker's yeast
    • Durchschlag, H., Biedermann, G., and Eggerer, H. 1981. Large-scale purification and some properties of malate synthase from baker's yeast. Eur. J. Biochem. 114: 255-262.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 255-262
    • Durchschlag, H.1    Biedermann, G.2    Eggerer, H.3
  • 17
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • Dym, O. and Eisenberg, D. 2001. Sequence-structure analysis of FAD-containing proteins. Protein Sci. 10: 1712-1728.
    • (2001) Protein Sci. , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 18
    • 0014102032 scopus 로고
    • The principle of catalysis of malate synthase
    • Eggerer, H. and Klette, A. 1967. The principle of catalysis of malate synthase. Eur. J. Biochem. 1: 447-475.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 447-475
    • Eggerer, H.1    Klette, A.2
  • 19
    • 0030444352 scopus 로고    scopus 로고
    • The diverse world of coenzyme A binding proteins
    • Engel, C. and Wierenga, R. 1996. The diverse world of coenzyme A binding proteins. Curr. Opin. Struct. Biol. 6: 790-797.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 790-797
    • Engel, C.1    Wierenga, R.2
  • 20
    • 0040941785 scopus 로고
    • Studies on specific enzyme inhibitors, VI: Characterization and mechanism of action of the enzyme-inhibitory isomer of monofluorocitrate
    • Fanshier. D.W., Gottwald, L.K., and Kun, E. 1964. Studies on specific enzyme inhibitors, VI: Characterization and mechanism of action of the enzyme-inhibitory isomer of monofluorocitrate. J. Biol. Chem. 239: 425-434.
    • (1964) J. Biol. Chem. , vol.239 , pp. 425-434
    • Fanshier, D.W.1    Gottwald, L.K.2    Kun, E.3
  • 21
    • 0034787623 scopus 로고    scopus 로고
    • Replacement of arginine-171 and aspartate-453 in Streptomyces coelicolor malate synthase A by site-directed mutagenesis inactivates the enzyme
    • Goh, L.L., Loke, P., and Sim, T.S. 2001. Replacement of arginine-171 and aspartate-453 in Streptomyces coelicolor malate synthase A by site-directed mutagenesis inactivates the enzyme. Appl. Microbiol. Biotech. 57: 363-367.
    • (2001) Appl. Microbiol. Biotech. , vol.57 , pp. 363-367
    • Goh, L.L.1    Loke, P.2    Sim, T.S.3
  • 22
    • 0033613213 scopus 로고    scopus 로고
    • Identification of Mycobacterium tuberculosis RNAs synthesized in response to phagocytosis by human macrophages by selective capture of transcribed sequences (SCOTS)
    • Graham, J.E. and Clark-Curtiss, J.E. 1999. Identification of Mycobacterium tuberculosis RNAs synthesized in response to phagocytosis by human macrophages by selective capture of transcribed sequences (SCOTS). Proc. Natl. Acad. Sci. 96: 11554-11559.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 11554-11559
    • Graham, J.E.1    Clark-Curtiss, J.E.2
  • 23
    • 0032884073 scopus 로고    scopus 로고
    • Expression of the soxR Gene of Pseudomonas aeruginosa is inducible during infection of burn wounds in mice and is required to cause efficient bacteremia
    • Ha, U. and Jin, S. 1999. Expression of the soxR Gene of Pseudomonas aeruginosa is inducible during infection of burn wounds in mice and is required to cause efficient bacteremia. Infect. Immun. 67: 5324-5331.
    • (1999) Infect. Immun. , vol.67 , pp. 5324-5331
    • Ha, U.1    Jin, S.2
  • 24
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • Hayward, S. and Berendsen, H.J. 1998. Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme. Proteins 30: 144-154.
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 25
    • 0344286166 scopus 로고    scopus 로고
    • Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis
    • Honer zu Bentrup, K., Miczak, A., Swenson, D.L., and Russell, D.G. 1999. Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis. J. Bacteriol. 181: 7161-7167.
    • (1999) J. Bacteriol. , vol.181 , pp. 7161-7167
    • Honer zu Bentrup, K.1    Miczak, A.2    Swenson, D.L.3    Russell, D.G.4
  • 26
    • 0034696680 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 Å resolution: Mechanistic implications
    • Howard, B.R., Endrizzi, J.A., and Remington, S.J. 2000. The crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 Å resolution: Mechanistic implications. Biochemistry 39: 3156-3168.
    • (2000) Biochemistry , vol.39 , pp. 3156-3168
    • Howard, B.R.1    Endrizzi, J.A.2    Remington, S.J.3
  • 27
    • 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., and Kjeldgaard, M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta. Crystallogr. A 47: 110.
    • (1991) Acta. Crystallogr. A , vol.47 , pp. 110
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0025214122 scopus 로고
    • Proposed mechanism for the condensation reaction of citrate synthase: 1. 9 Å structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A
    • Karpusas, M., Branchaud, B., and Remington, S.J. 1990. Proposed mechanism for the condensation reaction of citrate synthase: 1.9 Å structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A. Biochemistry 29: 2213-2219.
    • (1990) Biochemistry , vol.29 , pp. 2213-2219
    • Karpusas, M.1    Branchaud, B.2    Remington, S.J.3
  • 29
    • 0025923565 scopus 로고
    • 1.9 Å structures of ternary complexes of citrate synthase with D- and L-malate: Mechanistic implications
    • Karpusas, M., Holland, D., and Remington, S.J. 1991. 1.9 Å structures of ternary complexes of citrate synthase with D- and L-malate: Mechanistic implications. Biochemistry 30: 6024-6031.
    • (1991) Biochemistry , vol.30 , pp. 6024-6031
    • Karpusas, M.1    Holland, D.2    Remington, S.J.3
  • 30
    • 0019315271 scopus 로고
    • Synthesis of stereospecific deuterated fluoracetic acid and its behaviour in enzymic aldol-type condensations
    • Keck, R., Haas, H., and Retey, J. 1980. Synthesis of stereospecific deuterated fluoracetic acid and its behaviour in enzymic aldol-type condensations. FEBS Lett. 114: 287-290.
    • (1980) FEBS Lett. , vol.114 , pp. 287-290
    • Keck, R.1    Haas, H.2    Retey, J.3
  • 31
    • 0033081529 scopus 로고    scopus 로고
    • Rapid automated molecular replacement by evolutionary search
    • Kissinger, C.R., Gehlhaar, D.K., and Fogel, D.B. 1999. Rapid automated molecular replacement by evolutionary search. Acta Crystallogr. D 55: 484-491.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 484-491
    • Kissinger, C.R.1    Gehlhaar, D.K.2    Fogel, D.B.3
  • 32
    • 0000581636 scopus 로고
    • 2-units by a modified tricarboxylic acid cycle
    • 2-units by a modified tricarboxylic acid cycle. Nature 179: 988-991.
    • (1957) Nature , vol.179 , pp. 988-991
    • Kornberg, H.L.1    Krebs, H.A.2
  • 34
    • 0017099212 scopus 로고
    • Enzymic generation of chiral acetates: A quantitative evaluation of their configurational assay
    • Lenz, H. and Eggerer, H. 1976. Enzymic generation of chiral acetates: A quantitative evaluation of their configurational assay. Eur. J. Biochem. 65: 237-246.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 237-246
    • Lenz, H.1    Eggerer, H.2
  • 36
    • 0002414103 scopus 로고    scopus 로고
    • Molecular data processing
    • (eds. D. Moras, et al.). Oxford University Press. Oxford, UK
    • Leslie, A.G.W. 1996. Molecular data processing. In Crystallographic computing (eds. D. Moras, et al.), pp. 50-61. Oxford University Press. Oxford, UK.
    • (1996) Crystallographic Computing , pp. 50-61
    • Leslie, A.G.W.1
  • 37
    • 0035811478 scopus 로고    scopus 로고
    • The glyoxylate cycle is required for fungal virulence
    • Lorenz, M.C. and Fink, G.R. 2001. The glyoxylate cycle is required for fungal virulence. Nature 412: 83-86.
    • (2001) Nature , vol.412 , pp. 83-86
    • Lorenz, M.C.1    Fink, G.R.2
  • 38
    • 0014694549 scopus 로고
    • Preparation and detection of chiral methyl groups
    • Luthy, J., Retey, J., and Arigoni, D. 1969. Preparation and detection of chiral methyl groups. Nature 221: 1213-1215.
    • (1969) Nature , vol.221 , pp. 1213-1215
    • Luthy, J.1    Retey, J.2    Arigoni, D.3
  • 40
    • 0037118418 scopus 로고    scopus 로고
    • The arrangement of first-and second-sphere water molecules in divalent magnesium complexes: Results from molecular orbital and density functional theory and from structural crystallography
    • Markham, G.D., Glusker, J.P., and Bock, C.W. 2002. The arrangement of first-and second-sphere water molecules in divalent magnesium complexes: Results from molecular orbital and density functional theory and from structural crystallography. J. Phys. Chem. B 106: 5118-5134.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 5118-5134
    • Markham, G.D.1    Glusker, J.P.2    Bock, C.W.3
  • 41
    • 0019886922 scopus 로고
    • Sterochemical outcome of processing of fluorinated substrates by ATP citrate lyase and malate synthase
    • Marletta, M.A., Srere, P.A., and Walsh, C. 1981. Sterochemical outcome of processing of fluorinated substrates by ATP citrate lyase and malate synthase. Biochemistry 20: 3719-3723.
    • (1981) Biochemistry , vol.20 , pp. 3719-3723
    • Marletta, M.A.1    Srere, P.A.2    Walsh, C.3
  • 43
    • 37049073850 scopus 로고
    • Stereoelectronic effects of fluorine in enzyme chemistry. Stereospecific control of citrate synthase mediated synthesis of (2R,3R) 3-fluorocitrate by the relative stabilities of the intermediate fluoroenolates
    • O'Hagan, D. and Rzepa, H.S. 1994. Stereoelectronic effects of fluorine in enzyme chemistry. Stereospecific control of citrate synthase mediated synthesis of (2R,3R) 3-fluorocitrate by the relative stabilities of the intermediate fluoroenolates. J. Chem. Soc. Chem. Commun.: 2029-2030.
    • (1994) J. Chem. Soc. Chem. Commun. , pp. 2029-2030
    • O'Hagan, D.1    Rzepa, H.S.2
  • 44
    • 0029068129 scopus 로고
    • Isocitrate lyase activity in halophilic archaea
    • Oren, A. and Gurevich, P. 1995. Isocitrate lyase activity in halophilic archaea. FEMS Microbiol. Lett. 130: 91-95.
    • (1995) FEMS Microbiol. Lett. , vol.130 , pp. 91-95
    • Oren, A.1    Gurevich, P.2
  • 45
    • 0020483375 scopus 로고
    • Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution
    • Remington, S., Wiegand, G., and Huber, R. 1982. Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution. J. Mol. Biol. 158: 111-152.
    • (1982) J. Mol. Biol. , vol.158 , pp. 111-152
    • Remington, S.1    Wiegand, G.2    Huber, R.3
  • 46
    • 0000841544 scopus 로고
    • Mechanisms of citrate synthase and related enzymes (triose phosphate isomerase and mandelate racemase)
    • Remington, S.J. 1992. Mechanisms of citrate synthase and related enzymes (triose phosphate isomerase and mandelate racemase). Curr. Biol. 2: 730-735.
    • (1992) Curr. Biol. , vol.2 , pp. 730-735
    • Remington, S.J.1
  • 47
    • 0025048136 scopus 로고
    • The P-loop: A common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P.R., and Wittinghofer, A. 1990. The P-loop: A common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15: 430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 49
    • 0035975189 scopus 로고    scopus 로고
    • Sequencing, phylogenetic and transcriptional analysis of the glyoxylate bypass operon (ace) in the halophilic archaeon Haloferax volcanii
    • Serrano, J.A. and Bonete, M.J. 2001. Sequencing, phylogenetic and transcriptional analysis of the glyoxylate bypass operon (ace) in the halophilic archaeon Haloferax volcanii. Biochim. Biophys. Acta 1520: 154-162.
    • (2001) Biochim. Biophys. Acta , vol.1520 , pp. 154-162
    • Serrano, J.A.1    Bonete, M.J.2
  • 50
    • 0031688651 scopus 로고    scopus 로고
    • Operation of glyoxylate cycle in halophilic archaea: Presence of malate synthase and isocitrate lyase in Haloferax volcanii
    • Serrano, J.A., Camacho, M., and Bonete, M.J. 1998. Operation of glyoxylate cycle in halophilic archaea: Presence of malate synthase and isocitrate lyase in Haloferax volcanii. FEBS Lett. 434: 13-16.
    • (1998) FEBS Lett. , vol.434 , pp. 13-16
    • Serrano, J.A.1    Camacho, M.2    Bonete, M.J.3
  • 52
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud, D.E., Ten Eyck, L.F., and Matthews, B.W. 1987. An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Cryst. A43: 489-503.
    • (1987) Acta Cryst. A , vol.43 , pp. 489-503
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 53
    • 0037432547 scopus 로고    scopus 로고
    • Quantitative NMR studies of high molecular weight proteins: Application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G
    • Tugarinov, V. and Kay, L.E. 2003. Quantitative NMR studies of high molecular weight proteins: Application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G. J. Mol. Biol. 327: 1121-1133.
    • (2003) J. Mol. Biol. , vol.327 , pp. 1121-1133
    • Tugarinov, V.1    Kay, L.E.2
  • 54
    • 0037189901 scopus 로고    scopus 로고
    • Four-dimensional NMR spectroscopy of a 723-residue protein: Chemical shift assignments and secondary structure of malate synthase g
    • Tugarinov, V., Muhandiram, R., Ayed, A., and Kay, L.E. 2002. Four-dimensional NMR spectroscopy of a 723-residue protein: Chemical shift assignments and secondary structure of malate synthase g. J Am. Chem. Soc. 124: 10025-10035.
    • (2002) J Am. Chem. Soc. , vol.124 , pp. 10025-10035
    • Tugarinov, V.1    Muhandiram, R.2    Ayed, A.3    Kay, L.E.4
  • 55
    • 0037181133 scopus 로고    scopus 로고
    • Evidence for an operative glyoxylate cycle in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius
    • Uhrigshardt, H., Walden, M., John, H., Petersen, A., and Anemuller, S, 2002. Evidence for an operative glyoxylate cycle in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. FEBS Lett. 513: 223-229.
    • (2002) FEBS Lett. , vol.513 , pp. 223-229
    • Uhrigshardt, H.1    Walden, M.2    John, H.3    Petersen, A.4    Anemuller, S.5
  • 56
    • 0028241778 scopus 로고
    • A very short hydrogen bond provides only moderate stabilization of an enzyme-inhibitor complex of citrate synthase
    • Usher, K.C., Remington, S.J., Martin, D.P., and Drueckhammer, D.G. 1994. A very short hydrogen bond provides only moderate stabilization of an enzyme-inhibitor complex of citrate synthase. Biochemistry 33: 7753-7759.
    • (1994) Biochemistry , vol.33 , pp. 7753-7759
    • Usher, K.C.1    Remington, S.J.2    Martin, D.P.3    Drueckhammer, D.G.4
  • 58
    • 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., and Hol, W.G. 1986. Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187: 101-107.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.3
  • 59
    • 0028878767 scopus 로고
    • EDPDB: A multifunctional tool for protein structure analysis
    • Zhang, X.J. and Matthews, B.W. 1995. EDPDB: A multifunctional tool for protein structure analysis. J. Appl. Crystallogr. 28: 624-630.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 624-630
    • Zhang, X.J.1    Matthews, B.W.2
  • 60
    • 0017357698 scopus 로고
    • Small-angle X-ray studies on malate synthase from baker's yeast
    • Zipper, P. and Durchschlag, H. 1977. Small-angle X-ray studies on malate synthase from baker's yeast. Biochem. Biophys. Res. Commun. 75: 394-400.
    • (1977) Biochem. Biophys. Res. Commun. , vol.75 , pp. 394-400
    • Zipper, P.1    Durchschlag, H.2
  • 61
    • 12444344323 scopus 로고
    • Small angle X-ray scattering studies on the X-ray-induced aggregation of malate synthase II: Inactivation and aggregation experiments
    • -. 1981. Small angle X-ray scattering studies on the X-ray-induced aggregation of malate synthase II: Inactivation and aggregation experiments. Monatshefte für Chemie 112: 1-23.
    • (1981) Monatshefte für Chemie , vol.112 , pp. 1-23


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