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1m2x

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Revision as of 10:38, 20 March 2008 by OCA (Talk | contribs)
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PDB ID 1m2x

Drag the structure with the mouse to rotate
, resolution 1.5Å
Ligands: , , and
Gene: blaB (Elizabethkingia meningoseptica)
Activity: Beta-lactamase, with EC number 3.5.2.6
Coordinates: save as pdb, mmCIF, xml



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. 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 Thu Mar 20 12:38:15 2008

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