Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 60, Issue 8, Pages 1764-1773Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-003-3189-2
Keywords
class-C beta-lactamase; Enterobacter cloacae 908R; boronic acid complex; iodo-acetamido-phenyl boronic acid (IAPB); transition-state analogue
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The structures of the, class C beta-lactamase from Enterobacter cloacae 908R alone and in complex with a baronic acid transition-state analogue were determined by X-ray crystallography at 2.1 and 2.3 Angstrom, respectively. The structure of the enzyme resembles those of other class C beta-lactamases. The structure of the. complex with the transition-state analogue, iodo-acetamido-phenyl boronic acid, shows that the inhibitor is covalently, bound to the active-site serine (Ser64). Binding of the inhibitor within the active site is compared with previously determined structures of complexes with other class C enzymes. The structure of the boronic acid adduct indicates ways to improve the affinity of this class of inhibitors. This structure of 908R class C beta-lactamase in complex with a transitionstate analogue provides further insights into the mechanism of action of these hydrolases.
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