The structure of the dizinc subclass B2 metallo-beta-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site.

Abstract

Bacteria can defend themselves against beta-lactam antibiotics through the expression of class B beta-lactamases, which cleave the beta-lactam amide bond and render the molecule harmless. There are three subclasses of class B beta-lactamases (B1, B2, and B3), all of which require Zn2+ for activity and can bind either one or two zinc ions. Whereas the B1 and… (More)
DOI: 10.1128/AAC.00288-09

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Cite this paper

@article{Bebrone2009TheSO, title={The structure of the dizinc subclass B2 metallo-beta-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site.}, author={Carine Bebrone and Heinrich Delbr{\"u}ck and Micha{\"e}l B Kupper and Philipp Schl{\"o}mer and Charlotte A. Willmann and J. Fr{\`e}re and Rainer Fischer and Moreno Galleni and Kurt Max Hoffmann}, journal={Antimicrobial agents and chemotherapy}, year={2009}, volume={53 10}, pages={4464-71} }