Download MendeleyCrystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue.
Wouters, J., Fonze, E., Vermeire, M., Frere, J.M., Charlier, P.(2003) Cell Mol Life Sci 60: 1764-1773
- PubMed: 14521155
- DOI: https://doi.org/10.1007/s00018-003-3189-2
- Primary Citation of Related Structures:
1S6R - PubMed Abstract:
The structures of the class C beta-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 A, 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 transition-state analogue provides further insights into the mechanism of action of these hydrolases.
Organizational Affiliation:
Institut de Recherche Microbiologiques JM Wiame, Brussels, Belgium. jwouters@dbm.ulb.ac.be
