Garcia-Saez, I.; Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-Commissariat à l'Energie Atomique (CEA)-Université Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France
Docquier, Jean-Denis ; Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines
Rossolini, G. M.; Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Università degli Studi di Siena, I-53100 Siena, Italy
Dideberg, O.; Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-Commissariat à l'Energie Atomique (CEA)-Université Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France
Language :
English
Title :
The Three-Dimensional Structure of VIM-2, a Zn-β-Lactamase from Pseudomonas aeruginosa in Its Reduced and Oxidised Form
Ambler R.P. The structure of beta-lactamases. Philos. Trans. R. Soc. Lond., B Biol. Sci. 289 (1980) 321-331
Rasmussen B.A., and Bush K. Carbapenem-hydrolyzing beta-lactamases. Antimicrob. Agents Chemother. 41 (1997) 223-232
Senda K., Arakawa Y., Ichiyama S., Nakashima K., Ito H., Ohsuka S., et al. PCR detection of metallo-beta-lactamase gene (blaIMP) in gram-negative rods resistant to broad-spectrum beta-lactams. J. Clin. Microbiol. 34 (1996) 2909-2913
Walsh T.R. The emergence and implications of metallo-β-lactamases in Gram-negative bacteria. Clin. Microbiol. Infect. 11 (2005) 2-9
Walsh T.R., Toleman M.A., Poirel L., and Nordmann P. Metallo-β-lactamases: the quiet before the storm?. Clin. Microbiol. Rev. 18 (2005) 306-325
Watanabe M., Iyobe S., Inoue M., and Mitsuhashi S. Transferable imipenem resistance in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 35 (1991) 147-151
Hirakata Y., Izumikawa K., Yamaguchi T., Takemura H., Tanaka H., Yoshida R., et al. Rapid detection and evaluation of clinical characteristics of emerging multiple-drug-resistant gram-negative rods carrying the metallo-beta-lactamase gene blaIMP. Antimicrob. Agents Chemother. 42 (1998) 2006-2011
Lauretti L., Riccio M.L., Mazzariol A., Cornaglia G., Amicosante G., Fontana R., and Rossolini G.M. Cloning and characterization of blaVIM, a new integron-borne metallo-beta-lactamase gene from a Pseudomonas aeruginosa clinical isolate. Antimicrob. Agents Chemother. 43 (1999) 1584-1590
Poirel L., Naas T., Nicolas D., Collet L., Bellais S., Cavallo J.D., and Nordmann P. Characterization of VIM-2, a carbapenem-hydrolyzing metallo-beta-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France. Antimicrob. Agents Chemother. 44 (2000) 891-897
Poirel L., and Nordmann P. Acquired carbapenem-hydrolyzing beta-lactamases and their genetic support. Curr. Pharm. Biotechnol. 3 (2002) 117-127 (review)
Bush K. Metallo-beta-lactamases: a class apart. Clin. Infect. Dis. 27 (1998) 48-53
Galleni M., Lamotte-Brasseur J., Rossolini G.M., Spencer J., Dideberg O., and Frère J.M. Standard numbering scheme for class B beta-lactamases. Antimicrob. Agents Chemother. 45 (2001) 660-663
Garau G., Garcia-Saez I., Bebrone C., Anne C., Mercuri P., Galleni M., et al. Update of the standard numbering scheme for class B beta-lactamases. Antimicrob. Agents Chemother. 48 (2004) 2347-2349
Frère J.M., Galleni M., Bush K., and Dideberg O. Is it necessary to change the classification of β-lactamases?. J. Antimicrob. Chemother. 55 (2005) 1051-1053
Queenan A.M., and Bush K. Carbapenemases: the versatile β-lactamases. Clin. Microbiol. Rev. 20 (2007) 440-458
Livermore D.M., and Woodford N. The β-lactamase threat in Enterobacteriaceae, Pseudomonas and Acinetobacter. Trends Microbiol. 14 (2006) 413-420
Pallecchi L., Riccio M.L., Docquier J.D., Fontana R., and Rossolini G.M. Molecular heterogeneity of bla(VIM-2)-containing integrons from Pseudomonas aeruginosa plasmids encoding the VIM-2 metallo-beta-lactamase. FEMS Microbiol. Lett. 195 (2001) 145-150
Yan J.J., Hsueh P.R., Ko W.C., Luh K.T., Tsai S.H., Wu H.M., and Wu J.J. Metallo-beta-lactamases in clinical Pseudomonas isolates in Taiwan and identification of VIM-3, a novel variant of the VIM-2 enzyme. Antimicrob. Agents Chemother. 45 (2001) 2224-2228
Docquier J.D., Lamotte-Brasseur J., Galleni M., Amicosante G., Frere J.M., and Rossolini G.M. On functional and structural heterogeneity of VIM-type metallo-beta-lactamases. J. Antimicrob. Chemother. 51 (2003) 257-266
DeLano W.L. The PyMOL Molecular Graphics System (2002), DeLano Scientific, San Carlos, CA
Navaza J., and Saludjian P. AMoRe: an automated molecular replacement program package. Methods Enzymol. 276 (1997) 581-594
Carfi A., Duée E., Paul-Soto R., Galleni M., Frere J.M., and Dideberg O. 1.85 Å resolution structure of the Zinc (II) beta-lactamase from Bacillus cereus. Acta Crystallogr., Sect. D: Biol. Crystallogr. 54 (1998) 313-323
Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr., Sect. D: Biol. Crystallogr. 54 (1998) 905-921
Roussel A., and Cambillau C. The TURBO-FRODO graphics package. Silicon Graphics Geometry Partners Directory, Volume 81 (1991), Silicon Graphics, Mountain View, CA
Carfi A., Parès S., Duée E., Galleni M., Duez C., Frère J.M., and Dideberg O. The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14 (1995) 4914-4921
Scrofani S.D., Chung J., Huntley J.J., Benkovic S.J., Wright P.E., and Dyson H.J. NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop. Biochemistry 38 (1999) 14507-14514
Concha N.O., Janson C.A., Rowling P., Pearson S., Cheever C.A., Clarke B.P., et al. Crystal structure of the IMP-1 metallo-beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 39 (2000) 4288-4298
Huntley J.J., Scrofani S.D., Osborne M.J., Wright P.E., and Dyson H.J. Dynamics of the metallo-beta-lactamase from Bacteroides fragilis in the presence and absence of a tight-binding inhibitor. Biochemistry 39 (2000) 13356-13364
Salsbury Jr. F.R., Crowley M.F., and Brooks III C.L. Modeling of the metallo-beta-lactamase from B. fragilis: structural and dynamic effects of inhibitor binding. Proteins: Struct. Funct. Genet. 44 (2001) 448-459
Huntley J.J., Fast W., Benkovic S.J., Wright P.E., and Dyson H.J. Role of the solvent exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase. Protein Sci. 12 (2003) 1368-1375
Moali C., Anne C., Lamotte-Brasseur J., Groslambert S., Devreese B., Van Beeumen J., et al. Analysis of the importance of the metallo-beta-lactamase active site loop in substrate binding and catalysis. Chem. Biol. 10 (2003) 319-329
Otwinowsky Z., and Minor W. Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
Davies A.M., Rasia R.M., Vila A.J., Sutton B.J., and Fabiane S.M. Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism. Biochemistry 44 (2005) 4841-4849
Murphy T.A., Catto L.E., Halford S.E., Hadfield A.T., Minor W., Walsh T.R., and Spencer J. Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-β-lactamases. J. Mol. Biol. 357 (2006) 890-903
Ruzheinikov S.N., Das S.K., Sedelnikova S.E., Hartley A., Foster S.J., Horsburgh M.J., et al. The 1.2 Å structure of a novel quorum-sensing protein, Bacillus subtilis LuxS. J. Mol. Biol. 313 (2001) 111-122
Franceschini N., Caravelli B., Docquier J.D., Galleni M., Frère J.M., Amicosante G., et al. Purification and biochemical characterization of the VIM-1 metallo-β-lactamase. Antimicrob. Agents Chemother. 44 (2000) 891-897
Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
Concha N.O., Rasmussen B.A., Bush K., and Herzberg O. Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure 4 (1996) 823-836
Garcia-Saez I., Hopkins J., Papamicael C., Franceschini N., Amicosante G., Rossolini G.M., et al. The 1.5 Å structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, d-captopril. J. Biol. Chem. 278 (2003) 23868-23873
