3p98

The crystal structure of the extended spectrum beta-lactamase TEM-72 reveals inhibition by citrate

spinqualitylabelsall models 3p98, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3p98 is a 2 chain structure with sequence from Morganella morganii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: CIT, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9R429_MORMO Publication Abstract from PubMed TEM-72, a class A beta-lactamase identified in isolates of Enterobacteriaceae, is a quadruple mutant of TEM-1 (Q39K, M182T, G238S and E240K) and shows extended-spectrum beta-lactamase (ESBL) properties arising from the G238S and E240K substitutions. Although many structures of TEM variants have been published, they do not include an enzyme with the simultaneous presence of both of the ESBL-conferring G238S and E240K substitutions. Furthermore, the structure shows the presence of a citrate anion bound to the TEM-72 active site, where it interacts with all of the conserved residues of class A beta-lactamases. The present structure supports the use of polycarboxylates as a scaffold for the design of broad-spectrum inhibitors of serine beta-lactamases. Structure of the extended-spectrum beta-lactamase TEM-72 inhibited by citrate.,Docquier JD, Benvenuti M, Calderone V, Rossolini GM, Mangani S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt, 3):303-6. Epub 2011 Feb 18. PMID:21393831 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase 3D structures

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