1S6R

908R class c beta-lactamase bound to iodo-acetamido-phenyl boronic acid

Summary for 1S6R

• Entry DOI: 10.2210/pdb1s6r/pdb
• Related: 1KDS 3BLS
• Descriptor: beta-lactamase, 4-IODO-ACETAMIDO PHENYLBORONIC ACID (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Enterobacter cloacae
• Total number of polymer chains: 1
• Total formula weight: 39402.45

Authors

Wouters, J. (deposition date: 2004-01-27, release date: 2004-02-24, Last modification date: 2024-10-30)

Primary citation

Wouters, J.,Fonze, E.,Vermeire, M.,Frere, J.M.,Charlier, P.
Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue.
Cell.Mol.Life Sci., 60:1764-1773, 2003

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.

PubMed: 14521155
DOI: 10.1007/s00018-003-3189-2

Experimental method

X-RAY DIFFRACTION (2.24 Å)