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Volumn 14, Issue 12, 2007, Pages 1202-1206

Structure and dynamics of a molten globular enzyme

Author keywords

[No Author keywords available]

Indexed keywords

CHORISMATE MUTASE;

EID: 36849044219     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1325     Document Type: Article
Times cited : (96)

References (30)
  • 1
    • 0021570483 scopus 로고
    • Dynamics of proteins
    • Karplus, M. Dynamics of proteins. Adv. Biophys. 18, 165-190 (1984).
    • (1984) Adv. Biophys , vol.18 , pp. 165-190
    • Karplus, M.1
  • 2
    • 0037008011 scopus 로고    scopus 로고
    • Multiple conformational changes in enzyme catalysis
    • Hammes, G.G. Multiple conformational changes in enzyme catalysis. Biochemistry 41, 8221-8228 (2002).
    • (2002) Biochemistry , vol.41 , pp. 8221-8228
    • Hammes, G.G.1
  • 3
    • 33748619206 scopus 로고    scopus 로고
    • An NMR perspective on enzyme dynamics
    • Boehr, D.D., Dyson, H.J. & Wright, P.E. An NMR perspective on enzyme dynamics. Chem. Rev. 106, 3055-3079 (2006).
    • (2006) Chem. Rev , vol.106 , pp. 3055-3079
    • Boehr, D.D.1    Dyson, H.J.2    Wright, P.E.3
  • 5
    • 33646935697 scopus 로고    scopus 로고
    • Dynamical contributions to catalysis: Critical tests of a popular hypothesis
    • Olsson, M.H.M., Parson, W.W. & Warshel, A. Dynamical contributions to catalysis: critical tests of a popular hypothesis. Chem. Rev. 106, 1737-1756 (2006).
    • (2006) Chem. Rev , vol.106 , pp. 1737-1756
    • Olsson, M.H.M.1    Parson, W.W.2    Warshel, A.3
  • 6
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J. & Wright, P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6, 197-208 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 8
    • 0032516484 scopus 로고    scopus 로고
    • A small, thermostable, and monofunctional chorismate mutase from the archeon Methanococcus jannaschii
    • MacBeath, G., Kast, P. & Hilvert, D. A small, thermostable, and monofunctional chorismate mutase from the archeon Methanococcus jannaschii. Biochemistry 37, 10062-10073 (1998).
    • (1998) Biochemistry , vol.37 , pp. 10062-10073
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 9
    • 0032549781 scopus 로고    scopus 로고
    • Redesigning enzyme topology by directed evolution
    • MacBeath, G., Kast, P. & Hilvert, D. Redesigning enzyme topology by directed evolution. Science 279, 1958-1961 (1998).
    • (1998) Science , vol.279 , pp. 1958-1961
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 11
    • 33845377155 scopus 로고
    • An inhibitor of chorismate mutase resembling the transition-state conformation
    • Bartlett, P.A. & Johnson, C.R. An inhibitor of chorismate mutase resembling the transition-state conformation. J. Am. Chem. Soc. 107, 7792-7793 (1985).
    • (1985) J. Am. Chem. Soc , vol.107 , pp. 7792-7793
    • Bartlett, P.A.1    Johnson, C.R.2
  • 13
    • 0029109922 scopus 로고
    • Atomic structure of the buried catalytic pocket of Escherichia coli chorismate mutase
    • Lee, A.Y., Karplus, P.A., Ganem, B. & Clardy, J. Atomic structure of the buried catalytic pocket of Escherichia coli chorismate mutase. J. Am. Chem. Soc. 117, 3627-3628 (1995).
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 3627-3628
    • Lee, A.Y.1    Karplus, P.A.2    Ganem, B.3    Clardy, J.4
  • 14
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier, A. & Kay, L.E. New tools provide new insights in NMR studies of protein dynamics. Science 312, 224-228 (2006).
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 15
    • 33744908076 scopus 로고    scopus 로고
    • Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy
    • Palmer, A.G. & Massi, F. Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy. Chem. Rev. 106, 1700-1719 (2006).
    • (2006) Chem. Rev , vol.106 , pp. 1700-1719
    • Palmer, A.G.1    Massi, F.2
  • 16
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G. & Szabo, A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104, 4546-4559 (1982).
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 17
    • 33646911358 scopus 로고    scopus 로고
    • Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences
    • Jarymowycz, V.A. & Stone, M.J. Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences. Chem. Rev. 106, 1624-1671 (2006).
    • (2006) Chem. Rev , vol.106 , pp. 1624-1671
    • Jarymowycz, V.A.1    Stone, M.J.2
  • 18
    • 18244376600 scopus 로고    scopus 로고
    • Investigation of ligand binding and protein dynamics in Bacillus subtilis chorismate mutase by transverse relaxation optimized spectroscopy-nuclear magnetic resonance
    • Eletsky, A., Kienhöfer, A., Hilvert, D. & Pervushin, K. Investigation of ligand binding and protein dynamics in Bacillus subtilis chorismate mutase by transverse relaxation optimized spectroscopy-nuclear magnetic resonance. Biochemistry 44, 6788-6799 (2005).
    • (2005) Biochemistry , vol.44 , pp. 6788-6799
    • Eletsky, A.1    Kienhöfer, A.2    Hilvert, D.3    Pervushin, K.4
  • 20
    • 0014235891 scopus 로고
    • The catalytic and regulatory properties of enzymes
    • Koshland, D.E. & Neet, K.E. The catalytic and regulatory properties of enzymes. Annu. Rev. Biochem. 37, 359-410 (1968).
    • (1968) Annu. Rev. Biochem , vol.37 , pp. 359-410
    • Koshland, D.E.1    Neet, K.E.2
  • 21
    • 10944261243 scopus 로고    scopus 로고
    • Understanding noncovalent interactions: Ligand binding energy and catalytic efficiency from ligand-induced reductions in motion within receptors and enzymes
    • Williams, D.H., Stephens, E., O'Brien, D.P. & Zhou, M. Understanding noncovalent interactions: ligand binding energy and catalytic efficiency from ligand-induced reductions in motion within receptors and enzymes. Angew. Chem. Int. Ed. Engl. 43, 6596-6616 (2004).
    • (2004) Angew. Chem. Int. Ed. Engl , vol.43 , pp. 6596-6616
    • Williams, D.H.1    Stephens, E.2    O'Brien, D.P.3    Zhou, M.4
  • 22
    • 0016412390 scopus 로고
    • Energetics of ligand binding to proteins
    • Weber, G. Energetics of ligand binding to proteins. Adv. Protein Chem. 29, 1-83 (1975).
    • (1975) Adv. Protein Chem , vol.29 , pp. 1-83
    • Weber, G.1
  • 23
    • 15844385659 scopus 로고    scopus 로고
    • AutoLink: Automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization- based simulated logic
    • Masse, J.E. & Keller, R. AutoLink: automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization- based simulated logic. J. Magn. Reson. 174, 133-151 (2005).
    • (2005) J. Magn. Reson , vol.174 , pp. 133-151
    • Masse, J.E.1    Keller, R.2
  • 24
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Güntert, P. & Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319, 209-227 (2002).
    • (2002) J. Mol. Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 25
    • 0031304082 scopus 로고    scopus 로고
    • Automated combined assignment of NOESY spectra and three-dimensional protein structure determination
    • Mumenthaler, C., Güntert, P., Braun, W. & Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination. J. Biomol. NMR 10, 351-362 (1997).
    • (1997) J. Biomol. NMR , vol.10 , pp. 351-362
    • Mumenthaler, C.1    Güntert, P.2    Braun, W.3    Wüthrich, K.4
  • 27
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR protein structure calculation with CYANA
    • Güntert, P. Automated NMR protein structure calculation with CYANA. Meth. Mol. Biol. 278, 353-378 (2004).
    • (2004) Meth. Mol. Biol , vol.278 , pp. 353-378
    • Güntert, P.1
  • 29
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A.M., Akke, M. & Palmer, A.G. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 246, 144-163 (1995).
    • (1995) J. Mol. Biol , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 30
    • 0038068865 scopus 로고    scopus 로고
    • FAST-Modelfree: A program for rapid automated analysis of solution NMR spin-relaxation data
    • Cole, R. & Loria, J.P. FAST-Modelfree: a program for rapid automated analysis of solution NMR spin-relaxation data. J. Biomol. NMR 26, 203-213 (2003).
    • (2003) J. Biomol. NMR , vol.26 , pp. 203-213
    • Cole, R.1    Loria, J.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.