1s6r
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(New page: 200px<br /><applet load="1s6r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s6r, resolution 2.24Å" /> '''908R CLASS C BETA-LA...)
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Revision as of 21:51, 24 November 2007
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908R CLASS C BETA-LACTAMASE BOUND TO IODO-ACETAMIDO-PHENYL BORONIC ACID
Overview
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.
About this Structure
1S6R is a Single protein structure of sequence from Enterobacter cloacae with IAP as ligand. Active as Hydrolase, with EC number 3.5.2.6. Full crystallographic information is available from OCA.
Reference
Crystal 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 JM, Charlier P, Cell Mol Life Sci. 2003 Aug;60(8):1764-73. PMID:14521155
Page seeded by OCA on Sat Nov 24 23:59:06 2007
