Reference : Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-a...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/78085
Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue
English
Wouters, J. [> > > >]
Fonze, E. [> > > >]
Vermeire, M. [> > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Département des sciences de la vie >]
Charlier, Paulette mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Aug-2003
Cellular and Molecular Life Sciences
Birkhauser Verlag Ag
60
8
1764-1773
Yes (verified by ORBi)
International
1420-682X
Basel
[en] class-C beta-lactamase ; Enterobacter cloacae 908R ; boronic acid complex ; iodo-acetamido-phenyl boronic acid (IAPB) ; transition-state analogue
[en] 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.
http://hdl.handle.net/2268/78085

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