Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril
[en] The beta-lactamases are involved in bacterial resistance to penicillin and related compounds. Members of the metallo-enzyme class are now found in many pathogenic bacteria and are thus becoming of major clinical importance. The structures of the Zn-beta-lactamase from Fluoribacter gormanii (FEZ-1) in the native and in the complex form are reported here. FEZ-I is a monomeric enzyme, which possesses two zinc-binding sites. These structures are discussed in comparison with those of the tetrameric L1 enzyme produced by Stenotrophomonas maltophilia. From this analysis, amino acids involved in the oligomerization of L1 are clearly identified. Despite the similarity in fold, the active site of FEZ-1 was found to be significantly different. Two residues, which were previously implicated in function, are not present in L1 or in FEZ-1. The broad-spectrum substrate profile of Zn-beta-lactamases arises from the rather wide active-site cleft, where various P-lactam compounds can be accommodated. (C) 2003 Elsevier Science Ltd. All rights reserved.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Garcia-Saez, I.
Mercuri, Paola ; Université de Liège > Département des sciences de la vie > Macromolécules biologiques
Papamicael, C.
Kahn, R.
Frère, Jean-Marie ; Université de Liège - ULiège > Département des sciences de la vie > Département des sciences de la vie
Galleni, Moreno ; Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques
Rossolini, G. M.
Dideberg, O.
Language :
English
Title :
Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril
Publication date :
24 January 2003
Journal title :
Journal of Molecular Biology
ISSN :
0022-2836
eISSN :
1089-8638
Publisher :
Academic Press Ltd Elsevier Science Ltd, London, United Kingdom
Rasmussen B.A., Bush K. Carbapenem-hydrolyzing beta-lactamases. Antimicrob. Agents Chemother. 41:1997;223-232.
Arakawa Y., Murakami M., Suzuki K., Ito H., Wacharotayankun R., Ohsuka S., et al. A novel integron-like element carrying the metallo-beta-lactamase gene blaIMP. Antimicrob. Agents Chemother. 39:1995;1612-1615.
Lauretti L., Riccio M.L., Mazzariol A., Cornaglia G., Amicosante G., Fontana R., 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.
Bush K. Beta-Lactamases of increasing clinical importance. Curr. Pharm. Des. 5:1999;839-845.
Rasia R.M., Vila A.J. Exploring the role and the binding affinity of a second zinc equivalent in Bacillus cereus metallo-beta-lactamase. Biochemistry. 41:2002;1853-1860.
Wommer S., Rival S., Heinz U., Galleni M., Frère J.M., Franceschini N., et al. Substrate-activated zinc binding of metallo-beta-lactamases: physiological importance of the mononuclear enzymes. J. Biol. Chem. 277:2002;24142-24147.
Wang Z., Fast W., Benkovic S.J. On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis. Biochemistry. 38:1999;10013-10023.
Carfi A., Parès S., Duée E., Galleni M., Duez C., Frère J.M., 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.
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.
Galleni M., Lamotte-Brasseur J., Rossolini G.M., Spencer J., Dideberg O., Frere J.M. Standard numbering scheme for class B beta-lactamases. Antimicrob. Agents Chemother. 45:2001;660-663.
Boschi L., Mercuri P.S., Riccio M.L., Amicosante G., Galleni M., Frere J.M., Rossolini G.M. The legionella Fluoribacter gormanii metallo-beta-lactamase: a new member of the highly divergent lineage of molecular-subclass B3 beta-lactamases. Antimicrob. Agents Chemother. 44:2000;1538-1543.
Mercuri P.S., Bouillenne F., Boschi L., Lamotte-Brasseur J., Amicosante G., Devreese B., et al. Biochemical characterization of the FEZ-1 metallo-beta-lactamase of Legionella gormanii ATCC 33297(T) produced in Escherichia coli. Antimicrob. Agents Chemother. 45:2001;1254-1262.
Simm A.M., Higgins C.S., Pullan S.T., Avison M.B., Niumsup P., Erdozain O., et al. A novel metallo-beta-lactamase,Mbl1b, produced by the environmental bacterium Caulobacter crescentus. FEBS Letters. 509:2001;350-354.
Ullah J.H., Walsh T.R., Taylor I.A., Emery D.C., Verma C.S., Gamblin S.J., Spencer J. The crystal structure of the L1 Metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution. J. Mol. Biol. 284:1998;125-136.
Fitzgerald P.M.D., Wu J.K., Toney J.H. Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-Å resolution. Biochemistry. 37:1998;6791-6800.
Toney J.H., Hammond G.G., Fitzgerald P.M., Sharma N., Balkovec J.M., Rouen G.P., et al. Succinic acids as potent inhibitors of plasmid-borne imp-1 metallo-beta-lactamase. J. Biol. Chem. 276:2001;31913-31918.
Concha N.O., Rasmussen B.A., Bush K., Herzberg O. Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure. 4:1996;823-836.
Wang Z., Fast W., Valentine A.M., Benkovic S.J. Metallo-beta-lactamase: structure and mechanism. Curr. Opin. Chem. Biol. 3:1999;614-622.
Daiyasu H., Osaka K., Ishino Y., Toh H. Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold. FEBS Letters. 503:2001;1-6.
Suh J.T., Skiles J.W., Williams B.E., Youssefyeh R.D., Jones H., Loev B., et al. Angiotensin-converting enzyme-inhibitors-new orally active antihypertensive (mercaptoalkanoyl)-glycine and [(acylthio)alkanoyl] glycine derivatives. J. Med. Chem. 28:1985;57-66.
Skiles J.W., Suh J.T., Williams B.E., Menard P.R., Barton J.N., Loev B., et al. Angiotensin-converting enzyme-inhibitors-new orally active 1,4-thiazepine-2,5-diones, 1,4-thiazine-2,5-diones, and 1,4-benzothiazepine-2,5-diones possessing antihypertensive activity. J. Med. Chem. 29:1986;784-796.
Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallog. sect. D. 54:1998;905-921.
Miller R., Gallo S.M., Khalak H.G., Weeks C.M. SnB: crystal structure determination via Shake-and-Bake. J. Appl. Crystallog. 27:1994;613-662.
Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics. 15:1999;305-308.
Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallog. sect. D. 55:1999;938-940.