Crystal structure of Enterobacter cloacae 908R class C β-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue

J. Wouters, E. Fonzé, M. Vermeire, J. M. Frère, P. Charlier

Résultats de recherche: Contribution à un journal/une revueArticleRevue par des pairs

Résumé

The structures of the class C β-lactamase from Enterobacter cloacae 908R alone and in complex with a boronic acid transition-state analogue were determined by X-ray crystallography at 2.1 and 2.3 Å, respectively. The structure of the enzyme resembles those of other class C β-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 β-lactamase in complex with a transition-state analogue provides further insights into the mechanism of action of these hydrolases.

langue originaleAnglais
Pages (de - à)1764-1773
Nombre de pages10
journalCellular and Molecular Life Sciences
Volume60
Numéro de publication8
Les DOIs
Etat de la publicationPublié - 1 août 2003

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