3bls
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AMPC BETA-LACTAMASE FROM ESCHERICHIA COLI
OverviewOverview
The structures of AmpC beta-lactamase from Escherichia coli, alone and in, complex with a transition-state analogue, have been determined by X-ray, crystallography. The native enzyme was determined to 2.0 A resolution, and, the structure with the transition-state analogue m-aminophenylboronic acid, was determined to 2.3 A resolution. The structure of AmpC from E. coli, resembles those previously determined for the class C enzymes from, Enterobacter cloacae and Citrobacter freundii. The transition-state, analogue, m-aminophenylboronic acid, makes several interactions with AmpC, that were unexpected. Perhaps most surprisingly, the putative "oxyanion", of the boronic acid forms what appears to be a hydrogen bond with the, backbone carbonyl oxygen of Ala318, suggesting that this atom is, ... [(full description)]
About this StructureAbout this Structure
3BLS is a [Single protein] structure of sequence from [Escherichia coli] with APB as [ligand]. Active as [[1]], with EC number [3.5.2.6]. Full crystallographic information is available from [OCA].
ReferenceReference
Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design., Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ, Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:9819201
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