2cc1
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(New page: 200px<br /><applet load="2cc1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cc1, resolution 2.13Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 06:57, 21 November 2007
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CRYSTAL STRUCTURE OF THE CLASS A BETA-LACTAMASE FROM MYCOBACTERIUM FORTUITUM
Overview
beta-Lactamases are the main cause of bacterial resistance to penicillins, and cephalosporins. Class A beta-lactamases, the largest group of, beta-lactamases, have been found in many bacterial strains, including, mycobacteria, for which no beta-lactamase structure has been previously, reported. The crystal structure of the class A beta-lactamase from, Mycobacterium fortuitum (MFO) has been solved at 2.13-A resolution. The, enzyme is a chromosomally encoded broad-spectrum beta-lactamase with low, specific activity on cefotaxime. Specific features of the active site of, the class A beta-lactamase from M. fortuitum are consistent with its, specificity profile. Arg278 and Ser237 favor cephalosporinase activity and, could explain its broad substrate activity. The MFO active site presents, similarities with the CTX-M type extended-spectrum beta-lactamases but, lacks a specific feature of these enzymes, the VNYN motif (residues 103 to, 106), which confers on CTX-M-type extended-spectrum beta-lactamases a more, efficient cefotaximase activity.
About this Structure
2CC1 is a Single protein structure of sequence from [1]. This structure superseeds the now removed PDB entry 1MFO. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
Crystal structure of the Mycobacterium fortuitum class A beta-lactamase: structural basis for broad substrate specificity., Sauvage E, Fonze E, Quinting B, Galleni M, Frere JM, Charlier P, Antimicrob Agents Chemother. 2006 Jul;50(7):2516-21. PMID:16801434
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