1m2x
From Proteopedia
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Crystal Structure of the metallo-beta-lactamase BlaB of Chryseobacterium meningosepticum in complex with the inhibitor D-captopril
Overview
The crystal structure of the class-B beta-lactamase, BlaB, from the, pathogenic bacterium, Chryseobacterium meningosepticum, in complex with, the inhibitor, d-captopril, has been solved at 1.5-A resolution. The, enzyme has the typical alphabeta/betaalpha metallo-beta-lactamase fold and, the characteristic two metal binding sites of members of the subclass B1, in which two Zn2+ ions were identified. d-Captopril, a diastereoisomer of, the commercial drug, captopril, acts as an inhibitor by displacing the, catalytic hydroxyl ion required for antibiotic hydrolysis and, intercalating its sulfhydryl group between the two Zn2+ ions., Interestingly, d-captopril is located on one side of the active site, cleft. The x-ray structure of the complex of the closely related enzyme, IMP-1, with a mercaptocarboxylate inhibitor, which also contains a, sulfhydryl group bound to the two Zn2+ ions, shows the ligand to be, located on the opposite side of the active site cleft. A molecule, generated by fusion of these two inhibitors would cover the entire cleft, suggesting an interesting approach to the design of highly specific, inhibitors.
About this Structure
1M2X is a Single protein structure of sequence from Elizabethkingia meningoseptica with NA, ZN, MCO and GOL as ligands. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril., Garcia-Saez I, Hopkins J, Papamicael C, Franceschini N, Amicosante G, Rossolini GM, Galleni M, Frere JM, Dideberg O, J Biol Chem. 2003 Jun 27;278(26):23868-73. Epub 2003 Apr 8. PMID:12684522
Page seeded by OCA on Tue Nov 20 21:06:16 2007
