Structural basis for the interaction of lactivicins with serine beta-lactamases.

Anti-Bacterial Agents/chemistry; Bacillus/enzymology; Crystallography, X-Ray; Models, Molecular; Molecular Structure; Peptides/chemistry; Serine/metabolism; beta-Lactamases/chemistry/metabolism

Abstract :

[en] Lactivicin (LTV) is a natural non-beta-lactam antibiotic that inhibits penicillin-binding proteins and serine beta-lactamases. A crystal structure of a BS3-LTV complex reveals that, as for its reaction with PBPs, LTV reacts with the nucleophilic serine and that cycloserine and lactone rings of LTV are opened. This structure, together with reported structures of PBP1b with lactivicins, provides a basis for developing improved lactivicin-based gamma-lactam antibiotics.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Brown, Tom Jr

Charlier, Paulette ; Université de Liège - ULiège > Département des sciences de la vie > Cristallographie des macromolécules biologiques

Herman, Raphaël ; Université de Liège - ULiège > Centre d'ingénierie des protéines

Schofield, Christopher J

Sauvage, Eric ; Université de Liège - ULiège > Centre d'ingénierie des protéines

Language :

English

Title :

Structural basis for the interaction of lactivicins with serine beta-lactamases.

Publication date :

2010

Journal title :

Journal of Medicinal Chemistry

ISSN :

0022-2623

eISSN :

1520-4804

Publisher :

American Chemical Society, Washington, United States - District of Columbia

Volume :

Issue :

Pages :

5890-4

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 29 November 2010

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