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Volumn 50, Issue 48, 2011, Pages 10559-10565

Coenzyme a binding to the aminoglycoside acetyltransferase (3)-IIIb increases conformational sampling of antibiotic binding site

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDE ACETYLTRANSFERASE; ANTIBIOTIC BINDING; APO-ENZYMES; COENZYME A; DYNAMIC PROPERTY; DYNAMIC VARIATIONS; MOLECULAR DYNAMICS SIMULATIONS; STRUCTURAL CHANGE; STRUCTURAL FLEXIBILITIES;

EID: 82455219022     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201008f     Document Type: Article
Times cited : (10)

References (26)
  • 1
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • DOI 10.1038/327389a0
    • Moazed, D. and Noller, H. F. (1987) Interaction of antibiotics with functional sites in 16S ribosomal RNA Nature 327, 389-394 (Pubitemid 17075811)
    • (1987) Nature , vol.327 , Issue.6121 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 3
    • 0002881670 scopus 로고
    • Aminoglycoside-Aminocyclitol Antibiotics and Their Modifying Enzymes. Antibiotics in Laboratory Medicine
    • in, 4 th ed. (Davis, J. E. Ed.)
    • Lorian, V. (1991) Aminoglycoside-Aminocyclitol Antibiotics and Their Modifying Enzymes. Antibiotics in Laboratory Medicine, in Antibiotics in Laboratory Medicine, 4 th ed. (Davis, J. E., Ed.), p 1283.
    • (1991) Antibiotics in Laboratory Medicine , pp. 1283
    • Lorian, V.1
  • 4
    • 77952418687 scopus 로고    scopus 로고
    • Thermodynamics and Kinetics of Association of Antibiotics with the Aminoglycoside Acetyltransferase (3)-IIIb, a Resistance-Causing Enzyme
    • Norris, A. L., Özen, C., and Serpersu, E. H. (2010) Thermodynamics and Kinetics of Association of Antibiotics with the Aminoglycoside Acetyltransferase (3)-IIIb, a Resistance-Causing Enzyme Biochemistry 49, 4027-4035
    • (2010) Biochemistry , vol.49 , pp. 4027-4035
    • Norris, A.L.1    Özen, C.2    Serpersu, E.H.3
  • 5
    • 77952351391 scopus 로고    scopus 로고
    • Interactions of Coenzyme A with the Aminoglycoside Acetyltransferase (3)-IIIb and Thermodynamics of a Ternary System
    • Norris, A. L. and Serpersu, E. H. (2010) Interactions of Coenzyme A with the Aminoglycoside Acetyltransferase (3)-IIIb and Thermodynamics of a Ternary System Biochemistry 49, 4036-4042
    • (2010) Biochemistry , vol.49 , pp. 4036-4042
    • Norris, A.L.1    Serpersu, E.H.2
  • 6
    • 0030954208 scopus 로고    scopus 로고
    • GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein
    • DOI 10.1016/S0968-0004(97)01034-7, PII S0968000497010347
    • Neuwald, A. F. and Landsman, D. (1997) GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein Trends Biochem. Sci. 22, 154-155 (Pubitemid 27199313)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.5 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 7
    • 67650532852 scopus 로고    scopus 로고
    • NMR Detected Hydrogen-Deuterium Exchange Reveals Differential Dynamics of Antibiotic- and Nucleotide-Bound Aminoglycoside Phosphotransferase (3)-IIIa
    • Norris, A. L. and Serpersu, E. H. (2009) NMR Detected Hydrogen-Deuterium Exchange Reveals Differential Dynamics of Antibiotic- and Nucleotide-Bound Aminoglycoside Phosphotransferase (3)-IIIa J. Am. Chem. Soc. 131, 8587-8594
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8587-8594
    • Norris, A.L.1    Serpersu, E.H.2
  • 8
    • 0029400480 scopus 로고
    • Nmrpipe - A Multidimensional Spectral Processing System Based on Unix Pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) Nmrpipe-a Multidimensional Spectral Processing System Based on Unix Pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 12
    • 33748538349 scopus 로고    scopus 로고
    • Automatic atom type and bond type perception in molecular mechanical calculations
    • Wang, J., Wang, W., Kollman, P. A., and Case, D. A. (2006) Automatic atom type and bond type perception in molecular mechanical calculations J. Mol. Graphics Modell. 25, 247260
    • (2006) J. Mol. Graphics Modell. , vol.25 , pp. 247260
    • Wang, J.1    Wang, W.2    Kollman, P.A.3    Case, D.A.4
  • 14
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • Nosé, S. (1984) A unified formulation of the constant temperature molecular dynamics methods J. Chem. Phys. 81, 511-520
    • (1984) J. Chem. Phys. , vol.81 , pp. 511-520
    • Nosé, S.1
  • 15
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. G. (1985) Canonical dynamics: Equilibrium phase-space distributions Phys. Rev. A 31, 1695-1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 17
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • DOI 10.1063/1.328693
    • Parrinello, M. and Rahman, A. (1981) Polymorphic transitions in single crystals: A new molecular dynamics method J. Appl. Phys. 52, 7182-7190 (Pubitemid 12456820)
    • (1981) Journal of Applied Physics , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 19
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess, B., Kutzner, C., van der Spoel, D., and Lindahl, E. (2008) GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation J. Chem. Theory Comput. 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 20
    • 0346216028 scopus 로고    scopus 로고
    • Principal Components of the Protein Dynamical Transition
    • Tournier, A. L. and Smith, J. C. (2003) Principal Components of the Protein Dynamical Transition Phys. Rev. Lett. 91, 208106
    • (2003) Phys. Rev. Lett. , vol.91 , pp. 208106
    • Tournier, A.L.1    Smith, J.C.2
  • 21
    • 82455163218 scopus 로고    scopus 로고
    • Molecular Operating Environment (MOE), version 2010, The Chemical Computing Group, Montreal, Canada.
    • Molecular Operating Environment (MOE), version 2010, The Chemical Computing Group, Montreal, Canada.
  • 22
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity J. Am. Chem. Soc. 114, 10663-10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 23
    • 0032556228 scopus 로고    scopus 로고
    • Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments [10]
    • DOI 10.1021/ja982649y
    • Weigelt, J. (1998) Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments J. Am. Chem. Soc. 120, 10778-10779 (Pubitemid 28498833)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.41 , pp. 10778-10779
    • Weigelt, J.1
  • 24
    • 77951879659 scopus 로고    scopus 로고
    • Backbone resonance assignments of a promiscuous aminoglycoside antibiotic resistance enzyme; The aminoglycoside phosphotransferase(30)-IIIa
    • Serpersu, E. H., Özen, C., Norris, A. L., Steren, C., and Whittemore, N. (2010) Backbone resonance assignments of a promiscuous aminoglycoside antibiotic resistance enzyme; the aminoglycoside phosphotransferase(30)-IIIa Biomol. NMR Assignments 4, 9-12
    • (2010) Biomol. NMR Assignments , vol.4 , pp. 9-12
    • Serpersu, E.H.1    Özen, C.2    Norris, A.L.3    Steren, C.4    Whittemore, N.5
  • 25
    • 79956095443 scopus 로고    scopus 로고
    • ATP Binding Enables Broad Antibiotic Selectivity of Aminoglycoside phosphotransferase(3′)-IIIa: An Elastic Network Analysis
    • Wieninger, S. A., Serpersu, E. H., and Ullmann, G. M. (2011) ATP Binding Enables Broad Antibiotic Selectivity of Aminoglycoside phosphotransferase(3′)-IIIa: An Elastic Network Analysis J. Mol. Biol. 409, 450-465
    • (2011) J. Mol. Biol. , vol.409 , pp. 450-465
    • Wieninger, S.A.1    Serpersu, E.H.2    Ullmann, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.