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

Abstract:
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.
Publication status:
Published

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Publisher copy:
10.1021/jm100437u

Authors


Charlier, P More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Sauvage, E More by this author
Journal:
Journal of medicinal chemistry
Volume:
53
Issue:
15
Pages:
5890-5894
Publication date:
2010-08-05
DOI:
EISSN:
1520-4804
ISSN:
0022-2623
URN:
uuid:79be0f9e-2abc-472d-a3d1-88207e790fb1
Source identifiers:
60660
Local pid:
pubs:60660

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