3zgp | pdb_00003zgp

NMR structure of the catalytic domain from E. faecium L,D- transpeptidase acylated by ertapenem

spinqualitylabelsall models 3zgp Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zgp is a 1 chain structure with sequence from Enterococcus faecium. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1RG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3Y185_ENTFD Publication Abstract from PubMed The maintenance of bacterial cell shape and integrity is largely attributed to peptidoglycan, a biopolymer highly cross-linked through d,d-transpeptidation. Peptidoglycan cross-linking is catalyzed by penicillin-binding proteins (PBPs) that are the essential target of beta-lactam antibiotics. PBPs are functionally replaced by l,d-transpeptidases (Ldts) in ampicillin-resistant mutants of Enterococcus faecium and in wild-type Mycobacterium tuberculosis. Ldts are inhibited in vivo by a single class of beta-lactams, the carbapenems, which act as a suicide substrate. We present here the first structure of a carbapenem-acylated l,d-transpeptidase, E. faecium Ldtfm acylated by ertapenem, which revealed key contacts between the carbapenem core and residues of the catalytic cavity of the enzyme. Significant reorganization of the antibiotic conformation occurs upon enzyme acylation. These results, together with the analysis of protein-to-carbapenem proton transfers, provide new insights into the mechanism of Ldt acylation by carbapenems. Structure of Enterococcus faeciuml,d-Transpeptidase Acylated by Ertapenem Provides Insight into the Inactivation Mechanism.,Lecoq L, Dubee V, Triboulet S, Bougault C, Hugonnet JE, Arthur M, Simorre JP ACS Chem Biol. 2013 Apr 12. PMID:23574509 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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