Work

The Acylation Mechanism of CTX-M β-Lactamase at 0.88 Å Resolution

Year: 2007

Type: article

Abstract: The apo crystal structure of CTX-M-9 β-lactamase has been determined to 0.88 Å at pH 8.8. This unusually clear picture of proton positions and residue interactions supports the role of Glu166 as the general base for the controversial acylation step of class A β-lactamase catalysis. The ability to distinguish low-energy conformations sampled by the enzyme allows us to link the two conformations of Lys73 to different protonation states of Glu166.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja0712064

Authors: Yu Chen, Richard Bonnet, Brian K. Shoichet

Institution: University of California, San Francisco

Language: English

Topic: Antibiotic Resistance in Bacteria

Subfield: Molecular Medicine

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: G1250486013, Structure, Function and Inhibition of Beta-Lactamases