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

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
Pages (from-to)1764-1773
Number of pages10
JournalCellular and Molecular Life Sciences
Volume60
Issue number8
DOIs
Publication statusPublished - 1 Aug 2003

Keywords

  • Boronic acid complex
  • Class-C β-lactamase
  • Enterobacter cloacae 908R
  • Iodo-acetamido-phenyl boronic acid (IAPB)
  • Transition-state analogue

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