2x71 | pdb_00002x71

STRUCTURAL BASIS FOR THE INTERACTION OF LACTIVICINS WITH SERINE BETA-LACTAMASES

spinqualitylabelsall models 2x71, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x71 is a 2 chain structure with sequence from Bacillus licheniformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EOH, L4C, SO4 Activity: Beta-lactamase, with EC number 3.5.2.6 Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase

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