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Titolo:
Crystal structure of the class D beta-lactamase OXA-10
Autore:
Paetzel, M; Danel, F; de Castro, L; Mosimann, SC; Page, MGP; Strynadka, NCJ;
Indirizzi:
Univ British Columbia, Dept Biochem & Mol Biol, Vancouver, BC V6T 1Z3, Canada Univ British Columbia Vancouver BC Canada V6T 1Z3 ver, BC V6T 1Z3, Canada F Hoffmann La Roche & Co Ltd, Div Pharma, Preclin Res, CH-4070 Basel, Switzerland F Hoffmann La Roche & Co Ltd Basel Switzerland CH-4070 asel, Switzerland
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 10, volume: 7, anno: 2000,
pagine: 918 - 925
SICI:
1072-8368(200010)7:10<918:CSOTCD>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSITION-STATE ANALOG; CATALYTIC MECHANISM; CLASS-A; PSEUDOMONAS-AERUGINOSA; MOLECULAR-STRUCTURE; HYDROLYSIS; RESISTANCE; RESOLUTION; EVOLUTION; PHYLOGENY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Strynadka, NCJ Univ British Columbia, Dept Biochem & Mol Biol, 2146 Hlth Sci Mall, Vancouver, BC V6T 1Z3, Canada Univ British Columbia 2146 Hlth Sci Mall Vancouver BC Canada V6T 1Z3
Citazione:
M. Paetzel et al., "Crystal structure of the class D beta-lactamase OXA-10", NAT ST BIOL, 7(10), 2000, pp. 918-925

Abstract

We report the crystal structure of a class D beta-lactamase, the broad spectrum enzyme OXA-10 from Pseudomonas aeruginosa at 2.0 Angstrom resolution. There are significant differences between the overall fold observed in this structure and those of the evolutionarily related class A and class C beta-lactamases. Furthermore, the structure suggests the unique, cation mediated formation of a homodimer, Kinetic and hydrodynamic data shows that the dimer is a relevant species in solution and is the more active form of the enzyme. Comparison of the molecular details of the active sites of the classA and class C enzymes with the OXA-10 structure reveals that there is no counterpart in OXA-10 to the residues proposed to act as general bases in either of these enzymes (Glu 166 and Tyr 150. respectively). Our structures of the native and chloride inhibited forms of OXA-10 suggest that the class D enzymes have evolved a distinct catalytic mechanism for beta-lactam hydrolysis, Clinical variants of OXA-10 are also discussed in light of the structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 22:51:46