메뉴 건너뛰기




Volumn 57, Issue 2, 2013, Pages 848-854

Crystal structures of pseudomonas aeruginosa gim-1: Active-site plasticity in metallo-β-lactamases

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BACTERIAL ENZYME; CEFOXITIN; CYSTINE; GIM 1; HISTIDINE; ISOLEUCINE; LATAMOXEF; METALLO BETA LACTAMASE; SERINE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG; ZINC ION;

EID: 84872853235     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02227-12     Document Type: Article
Times cited : (21)

References (31)
  • 1
    • 0034780577 scopus 로고    scopus 로고
    • The development of ?-lactam antibiotics in response to the evolution of ?-lactamases
    • Essack SY. 2001. The development of ?-lactam antibiotics in response to the evolution of ?-lactamases. Pharm. Res. 18:1391-1399.
    • (2001) Pharm. Res. , vol.18 , pp. 1391-1399
    • Essack, S.Y.1
  • 2
    • 0036197034 scopus 로고    scopus 로고
    • Antibiotics: Action and resistance in gram-negative bacteria
    • Siu LK. 2002. Antibiotics: Action and resistance in gram-negative bacteria. J. Microbiol. Immunol. Infect. 35:1-11.
    • (2002) J. Microbiol. Immunol. Infect. , vol.35 , pp. 1-11
    • Siu, L.K.1
  • 3
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to ?-lactam antibiotics: Compelling opportunism, compelling opportunity
    • Fisher JF, Meroueh SO, Mobashery S. 2005. Bacterial resistance to ?-lactam antibiotics: Compelling opportunism, compelling opportunity. Chem. Rev. 105:395-424.
    • (2005) Chem. Rev. , vol.105 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 4
    • 78649697323 scopus 로고    scopus 로고
    • Emerging carbapenemases: A global perspective
    • Walsh TR. 2010. Emerging carbapenemases: A global perspective. Int. J. Antimicrob. Agents 36(Suppl. 3):S8-S14.
    • (2010) Int. J. Antimicrob. Agents , vol.36 , Issue.SUPPL. 3
    • Walsh, T.R.1
  • 7
    • 84869237356 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of an acquired subgroup B3 metallo-?-lactamase gene, blaAIM-1, and its unique genetic context in Pseudomonas aeruginosa from Australia
    • Yong D, Toleman MA, Bell J, Ritchie B, Pratt R, Ryley H, Walsh TR. 2012. Genetic and biochemical characterization of an acquired subgroup B3 metallo-?-lactamase gene, blaAIM-1, and its unique genetic context in Pseudomonas aeruginosa from Australia. Antimicrob. Agents Chemother. 56:6154-6159.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 6154-6159
    • Yong, D.1    Toleman, M.A.2    Bell, J.3    Ritchie, B.4    Pratt, R.5    Ryley, H.6    Walsh, T.R.7
  • 10
    • 9644289421 scopus 로고    scopus 로고
    • Molecular characterization of a ?-lactamase gene, blaGIM-1, encoding a new subclass of metallo-?-lactamase
    • Castanheira M, Toleman MA, Jones RN, Schmidt FJ, Walsh TR. 2004. Molecular characterization of a ?-lactamase gene, blaGIM-1, encoding a new subclass of metallo-?-lactamase. Antimicrob. Agents Chemother. 48: 4654-4661.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 4654-4661
    • Castanheira, M.1    Toleman, M.A.2    Jones, R.N.3    Schmidt, F.J.4    Walsh, T.R.5
  • 11
    • 84865416562 scopus 로고    scopus 로고
    • Emergence of metallo-?-lactamase GIM-1 in a clinical isolate of Serratia marcescens
    • Rieber H, Frontzek A, Pfeifer Y. 2012. Emergence of metallo-?-lactamase GIM-1 in a clinical isolate of Serratia marcescens. Antimicrob. Agents Chemother. 56:4945-4947.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 4945-4947
    • Rieber, H.1    Frontzek, A.2    Pfeifer, Y.3
  • 12
    • 84858629470 scopus 로고    scopus 로고
    • Emergence of metallo-?-lactamases GIM-1 and VIM in multidrug-resistant Pseudomonas aeruginosa in North Rhine-Westphalia, Germany
    • Rieber H, Frontzek A, von Baum H, Pfeifer Y. 2012. Emergence of metallo-?-lactamases GIM-1 and VIM in multidrug-resistant Pseudomonas aeruginosa in North Rhine-Westphalia, Germany. J. Antimicrob. Chemother. 67:1043-1045.
    • (2012) J. Antimicrob. Chemother. , vol.67 , pp. 1043-1045
    • Rieber, H.1    Frontzek, A.2    Von Baum, H.3    Pfeifer, Y.4
  • 14
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. 1993. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 24:795-800.
    • (1993) J. Appl. Crystallogr. , vol.24 , pp. 795-800
    • Kabsch, W.1
  • 20
    • 37349007671 scopus 로고    scopus 로고
    • The three-dimensional structure of VIM-2, a Zn-?-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form
    • Garcia-Saez I, Docquier JD, Rossolini GM, Dideberg O. 2008. The three-dimensional structure of VIM-2, a Zn-?-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form. J. Mol. Biol. 375:604-611.
    • (2008) J. Mol. Biol. , vol.375 , pp. 604-611
    • Garcia-Saez, I.1    Docquier, J.D.2    Rossolini, G.M.3    Dideberg, O.4
  • 21
    • 33644948482 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-?-lactamases
    • Murphy TA, Catto LE, Halford SE, Hadfield AT, Minor W, Walsh TR, Spencer J. 2006. Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-?-lactamases. J. Mol. Biol. 357:890-903.
    • (2006) J. Mol. Biol. , vol.357 , pp. 890-903
    • Murphy, T.A.1    Catto, L.E.2    Halford, S.E.3    Hadfield, A.T.4    Minor, W.5    Walsh, T.R.6    Spencer, J.7
  • 23
    • 15444376903 scopus 로고    scopus 로고
    • Effect of pH on the active site of an Arg121Cys mutant of the metallo-?-lactamase from Bacillus cereus: Implications for the enzyme mechanism
    • Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM. 2005. Effect of pH on the active site of an Arg121Cys mutant of the metallo-?-lactamase from Bacillus cereus: Implications for the enzyme mechanism. Biochemistry 44:4841-4849.
    • (2005) Biochemistry , vol.44 , pp. 4841-4849
    • Davies, A.M.1    Rasia, R.M.2    Vila, A.J.3    Sutton, B.J.4    Fabiane, S.M.5
  • 24
    • 10044225894 scopus 로고    scopus 로고
    • A metallo-?-lactamase enzyme in action: Crystal structures of the monozinc carbapenemase CphA and its complex with biapenem
    • Garau G, Bebrone C, Anne C, Galleni M, Frere JM, Dideberg O. 2005. A metallo-?-lactamase enzyme in action: Crystal structures of the monozinc carbapenemase CphA and its complex with biapenem. J. Mol. Biol. 345:785-795.
    • (2005) J. Mol. Biol. , vol.345 , pp. 785-795
    • Garau, G.1    Bebrone, C.2    Anne, C.3    Galleni, M.4    Frere, J.M.5    Dideberg, O.6
  • 25
    • 0034687116 scopus 로고    scopus 로고
    • Mutational analysis of metallo-?-lactamase CcrA from Bacteroides fragilis
    • Yanchak MP, Taylor RA, Crowder MW. 2000. Mutational analysis of metallo-?-lactamase CcrA from Bacteroides fragilis. Biochemistry 39: 11330-11339.
    • (2000) Biochemistry , vol.39 , pp. 11330-11339
    • Yanchak, M.P.1    Taylor, R.A.2    Crowder, M.W.3
  • 27
    • 7944238165 scopus 로고    scopus 로고
    • Analysis of the context dependent sequence requirements of active site residues in the metallo-?-lactamase IMP-1
    • Materon IC, Beharry Z, Huang W, Perez C, Palzkill T. 2004. Analysis of the context dependent sequence requirements of active site residues in the metallo-?-lactamase IMP-1. J. Mol. Biol. 344:653-663.
    • (2004) J. Mol. Biol. , vol.344 , pp. 653-663
    • Materon, I.C.1    Beharry, Z.2    Huang, W.3    Perez, C.4    Palzkill, T.5
  • 29
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas J, Ouyang Z, Tseng J, Binkowski A, Turpaz Y, Liang J. 2006. CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 34:W116-W118.
    • (2006) Nucleic Acids Res. , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 31
    • 70249131429 scopus 로고    scopus 로고
    • Positively cooperative binding of zinc ions to Bacillus cereus 569/H/9 ?-lactamase II suggests that the binuclear enzyme is the only relevant form for catalysis
    • Jacquin JO, Balbeur D, Damblon C, Marchot P, De Pauw E, Roberts GC, Frere JM, Matagne A. 2009. Positively cooperative binding of zinc ions to Bacillus cereus 569/H/9 ?-lactamase II suggests that the binuclear enzyme is the only relevant form for catalysis. J. Mol. Biol. 392:1278-1291.
    • (2009) J. Mol. Biol. , vol.392 , pp. 1278-1291
    • Jacquin, J.O.1    Balbeur, D.2    Damblon, C.3    Marchot, P.4    De Pauw, E.5    Roberts, G.C.6    Frere, J.M.7    Matagne, A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.