메뉴 건너뛰기




Volumn 585, Issue 2, 2011, Pages 364-368

The active site protonation states of perdeuterated Toho-1 β-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation

Author keywords

Lactamase; CTX M type ESBLs; Extended spectrum lactamases; Neutron diffraction; Perdeuterated neutron structure; Toho 1

Indexed keywords

ARGININE; ASPARAGINE; BETA LACTAMASE; BETA LACTAMASE TOHO 1; GLUTAMIC ACID; UNCLASSIFIED DRUG;

EID: 78651374505     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.12.017     Document Type: Article
Times cited : (33)

References (30)
  • 1
    • 0033082703 scopus 로고    scopus 로고
    • The β-lactamase cycle: A tale of selective pressure and bacterial ingenuity
    • DOI 10.1039/a705983c
    • A. Matagne, A. Dubus, M. Galleni, and J.M. Frere The beta-lactamase cycle: a tale of selective pressure and bacterial ingenuity Nat. Prod. Rep. 16 1 1999 1 19 (Pubitemid 29092067)
    • (1999) Natural Product Reports , vol.16 , Issue.1 , pp. 1-19
    • Matagne, A.1    Dubus, A.2    Galleni, M.3    Frere, J.-M.4
  • 2
    • 0347362476 scopus 로고    scopus 로고
    • Growing Group of Extended-Spectrum β-Lactamases: The CTX-M Enzymes
    • DOI 10.1128/AAC.48.1.1-14.2004
    • R. Bonnet Growing group of extended-spectrum beta-lactamases: the CTX-M enzymes Antimicrob. Agents Chemother. 48 1 2004 1 14 (Pubitemid 38040170)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.1 , pp. 1-14
    • Bonnet, R.1
  • 3
    • 0029121020 scopus 로고
    • Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A beta-lactamase isolated from Escherichia coli
    • Y. Ishii, A. Ohno, H. Taguchi, S. Imajo, M. Ishiguro, and H. Matsuzawa Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A beta-lactamase isolated from Escherichia coli Antimicrob. Agents Chemother. 39 1995 2269 2275
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2269-2275
    • Ishii, Y.1    Ohno, A.2    Taguchi, H.3    Imajo, S.4    Ishiguro, M.5    Matsuzawa, H.6
  • 4
    • 0041818050 scopus 로고    scopus 로고
    • Crystal structure of extended-spectrum β-lactamase Toho-1: Insights into the molecular mechanism for catalytic reaction and substrate specificity expansion
    • DOI 10.1021/bi0342822
    • A.S. Ibuka, Y. Ishii, M. Galleni, M. Ishiguro, K. Yamaguchi, J.M. Frere, H. Matsuzawa, and H. Sakai Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for catalytic reaction and substrate specificity expansion Biochemistry 42 36 2003 10634 10643 (Pubitemid 37102102)
    • (2003) Biochemistry , vol.42 , Issue.36 , pp. 10634-10643
    • Ibuka, A.S.1    Ishii, Y.2    Galleni, M.3    Ishiguro, M.4    Yamaguchi, K.5    Frere, J.-M.6    Matsuzawa, H.7    Sakai, H.8
  • 5
    • 0025647444 scopus 로고
    • Site-directed mutagenesis of beta-lactamase I. Single and double mutants of Glu-166 and Lys-73
    • R.M. Gibson, H. Christensen, and S.G. Waley Site-directed mutagenesis of beta-lactamase I. Single and double mutants of Glu-166 and Lys-73 Biochem. J. 272 1990 613 619
    • (1990) Biochem. J. , vol.272 , pp. 613-619
    • Gibson, R.M.1    Christensen, H.2    Waley, S.G.3
  • 6
    • 4544384195 scopus 로고    scopus 로고
    • The importance of a critical protonation state and the fate of the catalytic steps in class A β-lactamases and penicillin-binding proteins
    • DOI 10.1074/jbc.M313143200
    • D. Golemi-Kotra, S.O. Meroueh, C. Kim, S.B. Vakulenko, A. Bulychev, A.J. Stemmler, T.L. Stemmler, and S. Mobashery The importance of a critical protonation state and the fate of the catalytic steps in class A beta-lactamases and penicillin-binding proteins J. Biol. Chem. 279 2004 34665 34673 (Pubitemid 39318096)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34665-34673
    • Golemi-Kotra, D.1    Meroueh, S.O.2    Kim, C.3    Vakulenko, S.B.4    Bulychev, A.5    Stemmler, A.J.6    Stemmler, T.L.7    Mobashery, S.8
  • 9
    • 27644522933 scopus 로고    scopus 로고
    • Ab initio QM/MM study of class A β-lactamase acylation: Dual participation of Glu166 and Lys73 in a concerted base promotion of Ser70
    • DOI 10.1021/ja051592u
    • S.O. Meroueh, J.F. Fisher, H.B. Schlegel, and S. Mobashery Ab initio QM/MM study of class A beta-lactamase acylation: dual participation of Glu166 and Lys73 in a concerted base promotion of Ser70 J. Am. Chem. Soc. 127 2005 15397 15407 (Pubitemid 41572513)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.44 , pp. 15397-15407
    • Meroueh, S.O.1    Fisher, J.F.2    Schlegel, H.B.3    Mobashery, S.4
  • 10
    • 0042125389 scopus 로고    scopus 로고
    • Identification of Glu166 as the general base in the acylation reaction of class A, β-lactamases through QM/MM modeling
    • DOI 10.1021/ja034434g
    • J.C. Hermann, L. Ridder, A.J. Mulholland, and H.D. Holtje Identification of Glu166 as the general base in the acylation reaction of class A beta-lactamases through QM/MM modeling J. Am. Chem. Soc. 125 2003 9590 9591 (Pubitemid 36975913)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.32 , pp. 9590-9591
    • Hermann, J.C.1    Ridder, L.2    Mulholland, A.J.3    Holtje, H.-D.4
  • 11
    • 34247857459 scopus 로고    scopus 로고
    • The acylation mechanism of CTX-M β-lactamase at 0.88 A resolution
    • DOI 10.1021/ja0712064
    • Y. Chen, R. Bonnet, and B.K. Shoichet The acylation mechanism of CTX-M beta-lactamase at 0.88 A resolution J. Am. Chem. Soc. 129 17 2007 5378 5380 (Pubitemid 46697623)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.17 , pp. 5378-5380
    • Chen, Y.1    Bonnet, R.2    Shoichet, B.K.3
  • 12
    • 16244415566 scopus 로고    scopus 로고
    • Atomic resolution structures of CTX-M β-lactamases: Extended spectrum activities from increased mobility and decreased stability
    • DOI 10.1016/j.jmb.2005.02.010
    • Y. Chen, J. Delmas, J. Sirot, B. Shoichet, and R. Bonnet Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability J. Mol. Biol. 348 2005 349 362 (Pubitemid 40462101)
    • (2005) Journal of Molecular Biology , vol.348 , Issue.2 , pp. 349-362
    • Chen, Y.1    Delmas, J.2    Sirot, J.3    Shoichet, B.4    Bonnet, R.5
  • 14
    • 17644390560 scopus 로고    scopus 로고
    • Structure, function, and inhibition along the reaction coordinate of CTX-M β-lactamases
    • DOI 10.1021/ja042850a
    • Y. Chen, B. Shoichet, and R. Bonnet Structure, function, and inhibition along the reaction coordinate of CTX-M beta-lactamases J. Am. Chem. Soc. 127 2005 5423 5434 (Pubitemid 40569854)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.15 , pp. 5423-5434
    • Chen, Y.1    Shoichet, B.2    Bonnet, R.3
  • 15
    • 2242480185 scopus 로고    scopus 로고
    • Acyl-intermediate structures of the extended-spectrum class A β-lactamase, Toho-1, in complex with cefotaxime, cephalothin, and benzylpenicillin
    • DOI 10.1074/jbc.M207884200
    • T. Shimamura, A. Ibuka, S. Fushinobu, T. Wakagi, M. Ishiguro, Y. Ishii, and H. Matsuzawa Acyl-intermediate structures of the extended-spectrum class A beta-lactamase, Toho-1, in complex with cefotaxime, cephalothin, and benzylpenicillin J. Biol. Chem. 277 48 2002 46601 46608 (Pubitemid 35417659)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 46601-46608
    • Shimamura, T.1    Ibuka, A.2    Fushinobu, S.3    Wakagi, T.4    Ishiguro, M.5    Ishii, Y.6    Matsuzaw, H.7
  • 16
    • 76849096440 scopus 로고    scopus 로고
    • The catalytic efficiency (k(cat)/K(m)) of the class A beta-lactamase Toho-1 correlates with the thermal stability of its catalytic intermediate analog
    • Y. Nitanai, T. Shimamura, T. Uchiyama, Y. Ishii, M. Takehira, K. Yutan, H. Matsuzawa, M. Miyano, and Biochim.Biophys. Acta The catalytic efficiency (k(cat)/K(m)) of the class A beta-lactamase Toho-1 correlates with the thermal stability of its catalytic intermediate analog Biochim. Biophys. Acta 1804 4 2010 684 691
    • (2010) Biochim. Biophys. Acta , vol.1804 , Issue.4 , pp. 684-691
    • Nitanai, Y.1    Shimamura, T.2    Uchiyama, T.3    Ishii, Y.4    Takehira, M.5    Yutan, K.6    Matsuzawa, H.7    Miyano, M.8    Acta, B..Biophys.9
  • 17
    • 77649270363 scopus 로고    scopus 로고
    • Neutron diffraction studies of a class A (-lactamase Toho-1 E166A/R274N/R276N triple mutant
    • S.J. Tomanicek, M.P. Blakeley, J. Cooper, Y. Chen, P.V. Afonine, and L. Coates Neutron diffraction studies of a class A (-lactamase Toho-1 E166A/R274N/R276N triple mutant J. Mol. Biol. 396 2010 1070 1080
    • (2010) J. Mol. Biol. , vol.396 , pp. 1070-1080
    • Tomanicek, S.J.1    Blakeley, M.P.2    Cooper, J.3    Chen, Y.4    Afonine, P.V.5    Coates, L.6
  • 18
    • 0037094114 scopus 로고    scopus 로고
    • An ultrahigh resolution structure of TEM-1 β-lactamase suggests a role for Glu166 as the general base in acylation
    • DOI 10.1021/ja0259640
    • G. Minasov, X. Wang, and B.K. Shoichet An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation J. Am. Chem. Soc. 124 2002 5333 5340 (Pubitemid 34506930)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.19 , pp. 5333-5340
    • Minasov, G.1    Wang, X.2    Shoichet, B.K.3
  • 19
    • 0037453313 scopus 로고    scopus 로고
    • Ultrahigh resolution structure of a class A β-lactamase: On the mechanism and specificity of the extended-spectrum SHV-2 enzyme
    • DOI 10.1016/S0022-2836(03)00210-9
    • M. Nukaga, K. Mayama, A.M. Hujer, R.A. Bonomo, and J.R. Knox Ultrahigh resolution structure of a class A beta-lactamase: on the mechanism and specificity of the extended-spectrum SHV-2 enzyme J. Mol. Biol. 328 2003 289 301 (Pubitemid 36390296)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.1 , pp. 289-301
    • Nukaga, M.1    Mayama, K.2    Hujer, A.M.3    Bonomo, R.A.4    Knox, J.R.5
  • 20
    • 0028237904 scopus 로고
    • Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing third-generation cephalosporins
    • W.A. Escobar, A.K. Tan, E.R. Lewis, and A.L. Fink Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing third-generation cephalosporins Biochemistry 33 1994 7619 7626
    • (1994) Biochemistry , vol.33 , pp. 7619-7626
    • Escobar, W.A.1    Tan, A.K.2    Lewis, E.R.3    Fink, A.L.4
  • 21
    • 0034595379 scopus 로고    scopus 로고
    • Lysine-73 is involved in the acylation and deacylation of β-lactamase
    • DOI 10.1021/bi992681k
    • E.J. Lietz, H. Truher, D. Kahn, M.J. Hokenson, and A.L. Fink Lysine-73 is involved in the acylation and deacylation of beta-lactamase Biochemistry 39 2000 4971 4981 (Pubitemid 30241616)
    • (2000) Biochemistry , vol.39 , Issue.17 , pp. 4971-4981
    • Lietz, E.J.1    Truher, H.2    Kahn, D.3    Hokenson, M.J.4    Fink, A.L.5
  • 23
    • 70449585313 scopus 로고    scopus 로고
    • Neutron macromolecular crystallography
    • M.P. Blakeley Neutron macromolecular crystallography Crystallogr. Rev. 15 3 2009 157 218
    • (2009) Crystallogr. Rev. , vol.15 , Issue.3 , pp. 157-218
    • Blakeley, M.P.1
  • 24
  • 25
    • 70350787183 scopus 로고    scopus 로고
    • Deuterium labeling for neutron structure-function-dynamics analysis
    • F. Meilleur, K.L. Weiss, and D.A.A. Myles Deuterium labeling for neutron structure-function-dynamics analysis Methods Mol. Biol. 544 2009 281 292
    • (2009) Methods Mol. Biol. , vol.544 , pp. 281-292
    • Meilleur, F.1    Weiss, K.L.2    Myles, D.A.A.3
  • 29
    • 21644480798 scopus 로고    scopus 로고
    • Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM β-lactamase
    • DOI 10.1021/bi0502700
    • V.L. Thomas, D. Golemi-Kotra, C. Kim, S.B. Vakulenko, S. Mobashery, and B.K. Shoichet Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM beta-lactamase Biochemistry 44 2005 9330 9338 (Pubitemid 40934383)
    • (2005) Biochemistry , vol.44 , Issue.26 , pp. 9330-9338
    • Thomas, V.L.1    Golemi-Kotra, D.2    Kim, C.3    Vakulenko, S.B.4    Mobashery, S.5    Shoichet, B.K.6
  • 30
    • 16244412269 scopus 로고    scopus 로고
    • Mechanisms of antibiotic resistance: QM/MM modeling of the acylation reaction of a class A β-lactamase with benzylpenicillin
    • DOI 10.1021/ja044210d
    • J.C. Hermann, C. Hensen, L. Ridder, A.J. Mulholland, and H.D. Holtje Mechanisms of antibiotic resistance. QM/MM modeling of the acylation reaction of a class A beta-lactamase with benzylpenicillin J. Am. Chem. Soc. 127 2005 4454 4465 (Pubitemid 40463071)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.12 , pp. 4454-4465
    • Hermann, J.C.1    Hensen, C.2    Ridder, L.3    Mulholland, A.J.4    Holtje, H.-D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.