Structural highlights
FunctionBLO1_KLEOX Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins. 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 PubMedKlebsiella oxytoca is a pathogen that causes serious infections in hospital patients. It shows resistance to many clinically used beta-lactam antibiotics by producing chromosomally encoded OXY-family beta-lactamases. Here, the crystal structure of an OXY-family beta-lactamase, OXY-1-1, determined at 1.93 A resolution is reported. The structure shows that the OXY-1-1 beta-lactamase has a typical class A beta-lactamase fold and exhibits greater similarity to CTX-M-type beta-lactamases than to TEM-family or SHV-family beta-lactamases. It is also shown that the enzyme provides more space around the active cavity for the R(1) and R(2) substituents of beta-lactam antibiotics. The half-positive/half-negative distribution of surface electrostatic potential in the substrate-binding pocket indicates the preferred properties of substrates or inhibitors of the enzyme. The results reported here provide a structural basis for the broadened substrate profile of the OXY-family beta-lactamases. Structural insights into the broadened substrate profile of the extended-spectrum beta-lactamase OXY-1-1 from Klebsiella oxytoca.,Liang YH, Gao R, Su XD Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1460-7. doi:, 10.1107/S090744491203466X. Epub 2012 Oct 18. PMID:23090395[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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