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Volumn 11, Issue 12, 2003, Pages 1499-1511

The Structure of Chorismate Synthase Reveals a Novel Flavin Binding Site Fundamental to a Unique Chemical Reaction

Author keywords

[No Author keywords available]

Indexed keywords

3 PHOSPHOSHIKIMATE 1 CARBOXYVINYLTRANSFERASE; AMINO ACID; ANTIFUNGAL AGENT; ANTIINFECTIVE AGENT; ANTIPROTOZOAL AGENT; CHORISMIC ACID; ENZYME; FLAVINE MONONUCLEOTIDE; HERBICIDE; SHIKIMIC ACID; SYNTHETASE; TETRAMER;

EID: 0344868502     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.11.005     Document Type: Article
Times cited : (52)

References (37)
  • 2
    • 0029743937 scopus 로고    scopus 로고
    • The transient kinetics of Escherichia coli chorismate synthase: Substrate consumption, product formation, phosphate dissociation, and characterization of a flavin intermediate
    • a
    • Bornemann S., Lowe D.J., Thorneley R.N.F. The transient kinetics of Escherichia coli chorismate synthase. substrate consumption, product formation, phosphate dissociation, and characterization of a flavin intermediate Biochemistry. 35:1996;9907-9916. a.
    • (1996) Biochemistry , vol.35 , pp. 9907-9916
    • Bornemann, S.1    Lowe, D.J.2    Thorneley, R.N.F.3
  • 4
    • 0036919327 scopus 로고    scopus 로고
    • Flavoenzymes that catalyse reactions with no net redox change
    • Bornemann S. Flavoenzymes that catalyse reactions with no net redox change. Nat. Prod. Rep. 19:2002;761-772.
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 761-772
    • Bornemann, S.1
  • 5
    • 0032537722 scopus 로고    scopus 로고
    • Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis
    • Carpenter E.P., Hawkins A.R., Frost J.W., Brown K.A. Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. Nature. 394:1998;299-302.
    • (1998) Nature , vol.394 , pp. 299-302
    • Carpenter, E.P.1    Hawkins, A.R.2    Frost, J.W.3    Brown, K.A.4
  • 6
    • 23544476001 scopus 로고
    • The CCP4 (Collaborative Computational Project 4) suite: Programs for protein crystallography
    • CCP4 The CCP4 (Collaborative Computational Project 4) suite. programs for protein crystallography Acta Crystallogr. D. Biol. Crystallogr. 55:1994;849-861.
    • (1994) Acta Crystallogr. D. Biol. Crystallogr. , vol.55 , pp. 849-861
  • 7
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:1988;10881-10890.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 8
    • 0035961045 scopus 로고    scopus 로고
    • A theoretical study of the chorismate synthase reaction
    • Dmitrenko O., Wood H.B. Jr., Bach R.D., Ganem B. A theoretical study of the chorismate synthase reaction. Org. Lett. 3:2001;4137-4140.
    • (2001) Org. Lett. , vol.3 , pp. 4137-4140
    • Dmitrenko, O.1    Wood, H.B.Jr.2    Bach, R.D.3    Ganem, B.4
  • 9
    • 0032612240 scopus 로고    scopus 로고
    • Flavoenzyme structure and function
    • S.K. Chapman, & G.A. Reid. Totowa, NJ: Humana press
    • Edmondson D., Ghisla S. Flavoenzyme structure and function. Chapman S.K., Reid G.A. Flavoprotein Protocols. 1999;157-179 Humana press, Totowa, NJ.
    • (1999) Flavoprotein Protocols , pp. 157-179
    • Edmondson, D.1    Ghisla, S.2
  • 12
    • 0005948379 scopus 로고
    • Stereochemistry of 1,4-conjugate elimination reactions
    • Hill R.K., Bock M.G. Stereochemistry of 1,4-conjugate elimination reactions. J. Am. Chem. Soc. 100:1978;637-639.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 637-639
    • Hill, R.K.1    Bock, M.G.2
  • 14
    • 0035900664 scopus 로고    scopus 로고
    • Spectroscopic and kinetic characterization of the bifunctional chorismate synthase from Neurospora crassa
    • Kitzing K., Macheroux P., Amrhein N. Spectroscopic and kinetic characterization of the bifunctional chorismate synthase from Neurospora crassa. J. Biol. Chem. 276:2001;42658-42666.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42658-42666
    • Kitzing, K.1    MacHeroux, P.2    Amrhein, N.3
  • 15
    • 0032557708 scopus 로고    scopus 로고
    • The three-dimensional structure of shikimate kinase
    • Krell T., Coggins J.R., Lapthorn A.J. The three-dimensional structure of shikimate kinase. J. Mol. Biol. 278:1998;983-997.
    • (1998) J. Mol. Biol. , vol.278 , pp. 983-997
    • Krell, T.1    Coggins, J.R.2    Lapthorn, A.J.3
  • 18
    • 0028102860 scopus 로고
    • Substrate analogs as mechanistic probes for the bifunctional chorismate synthase from Neurospora crassa
    • Lauhon C.T., Bartlett P.A. Substrate analogs as mechanistic probes for the bifunctional chorismate synthase from Neurospora crassa. Biochemistry. 33:1994;14100-14108.
    • (1994) Biochemistry , vol.33 , pp. 14100-14108
    • Lauhon, C.T.1    Bartlett, P.A.2
  • 19
    • 0032725979 scopus 로고    scopus 로고
    • Crystal structure of reduced thioredoxin reductase from Escherichia coli: Structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor
    • Lennon B.W., Williams C.H. Jr., Ludwig M.L. Crystal structure of reduced thioredoxin reductase from Escherichia coli. structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor Protein Sci. 8:1999;2366-2379.
    • (1999) Protein Sci. , vol.8 , pp. 2366-2379
    • Lennon, B.W.1    Williams, C.H.Jr.2    Ludwig, M.L.3
  • 20
    • 0039843614 scopus 로고    scopus 로고
    • Chemical modification of amino acid side chains
    • N.C. Price. Oxford, UK: Bios Scientific Publishing. , pp. 287-298
    • Lundblad R. Chemical modification of amino acid side chains. Price N.C. Proteins Labfax. 1996;Bios Scientific Publishing, Oxford, UK. , pp. 287-298.
    • (1996) Proteins Labfax
    • Lundblad, R.1
  • 21
    • 0029967883 scopus 로고    scopus 로고
    • Studies with flavin analogues provide evidence that a protonated reduce FMN is the substrate-induced transient intermediate in the reaction of Escherichia coli chorismate synthase
    • a
    • Macheroux P., Bornemann S., Ghisla S., Thorneley R.N.F. Studies with flavin analogues provide evidence that a protonated reduce FMN is the substrate-induced transient intermediate in the reaction of Escherichia coli chorismate synthase. J. Biol. Chem. 271:1996;25850-25856. a.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25850-25856
    • MacHeroux, P.1    Bornemann, S.2    Ghisla, S.3    Thorneley, R.N.F.4
  • 22
    • 0030065765 scopus 로고    scopus 로고
    • Binding of the oxidized, reduced and radical flavin species to chorismate synthase. An investigation by spectrophotometry, fluorimetry and electron paramagnetic resonance and electron double resonance spectroscopy
    • b
    • Macheroux P., Petersen J., Bornemann S., Lowe D.J., Thorneley R.N.F. Binding of the oxidized, reduced and radical flavin species to chorismate synthase. An investigation by spectrophotometry, fluorimetry and electron paramagnetic resonance and electron double resonance spectroscopy. Biochemistry. 35:1996;1643-1652. b.
    • (1996) Biochemistry , vol.35 , pp. 1643-1652
    • MacHeroux, P.1    Petersen, J.2    Bornemann, S.3    Lowe, D.J.4    Thorneley, R.N.F.5
  • 24
    • 0032944057 scopus 로고    scopus 로고
    • A unique reaction in a common pathway: Mechanism and function of chorismate synthase in the shikimate pathway
    • Macheroux P., Schmid J., Amrhein N., Schaller A. A unique reaction in a common pathway. mechanism and function of chorismate synthase in the shikimate pathway Planta. 207:1999;325-334.
    • (1999) Planta , vol.207 , pp. 325-334
    • MacHeroux, P.1    Schmid, J.2    Amrhein, N.3    Schaller, A.4
  • 25
    • 0028838717 scopus 로고
    • Threading a database of protein cores
    • Madej T., Gibrat J.-F., Bryant S.H. Threading a database of protein cores. Proteins. 23:1995;356-369.
    • (1995) Proteins , vol.23 , pp. 356-369
    • Madej, T.1    Gibrat, J.-F.2    Bryant, S.H.3
  • 26
    • 0038265866 scopus 로고    scopus 로고
    • Structures of shikimate dehydrogenase AroE and its paralog YdiB: A common structural framework for different activities
    • Michel G., Roszak A.W., Sauvé V., Maclean J., Matte A., Coggins J.R., Cygler M., Lapthorn A.J. Structures of shikimate dehydrogenase AroE and its paralog YdiB. a common structural framework for different activities J. Biol. Chem. 278:2003;19463-19472.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19463-19472
    • Michel, G.1    Roszak, A.W.2    Sauvé, V.3    MacLean, J.4    Matte, A.5    Coggins, J.R.6    Cygler, M.7    Lapthorn, A.J.8
  • 30
    • 0034680841 scopus 로고    scopus 로고
    • Studies with substrate and cofactor analogues provide evidence for a radical mechanism in the chorismate synthase reaction
    • Osborne A., Thorneley R.N.F., Abell C., Bornemann S. Studies with substrate and cofactor analogues provide evidence for a radical mechanism in the chorismate synthase reaction. J. Biol. Chem. 275:2000;35825-35830.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35825-35830
    • Osborne, A.1    Thorneley, R.N.F.2    Abell, C.3    Bornemann, S.4
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Jr. Carter, & R.M. Sweet. New York: Academic Press
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Carter C.W. Jr., Sweet R.M. Methods Enzymol. Volume 276. Macromolecular Crystallography Part A:1997;307-326 Academic Press, New York.
    • (1997) Methods Enzymol. Volume 276: Macromolecular Crystallography Part a , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I.N., Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11:1998;739-747.
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 35
    • 0033565448 scopus 로고    scopus 로고
    • The three dimensional structure of the phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli
    • Shumilin I., Kretsinger R., Bauerle R. The three dimensional structure of the phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. Structure. 7:1999;865-875.
    • (1999) Structure , vol.7 , pp. 865-875
    • Shumilin, I.1    Kretsinger, R.2    Bauerle, R.3
  • 37
    • 0028181528 scopus 로고
    • Protein classification by stochastic modeling and optimal filtering of amino-acid sequences
    • White J.V., Stultz C.M., Smith T.F. Protein classification by stochastic modeling and optimal filtering of amino-acid sequences. Math. Biosci. 119:1994;35-75.
    • (1994) Math. Biosci. , vol.119 , pp. 35-75
    • White, J.V.1    Stultz, C.M.2    Smith, T.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.