Structural highlights
Function
P94458_BACLI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural Basis for the Interaction of Lactivicins with Serine beta-Lactamases.,Brown T, Charlier P, Herman R, Schofield CJ, Sauvage E J Med Chem. 2010 Jul 1. PMID:20593835[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Brown T, Charlier P, Herman R, Schofield CJ, Sauvage E. Structural Basis for the Interaction of Lactivicins with Serine beta-Lactamases. J Med Chem. 2010 Jul 1. PMID:20593835 doi:10.1021/jm100437u
