2bls
From Proteopedia
| Line 23: | Line 23: | ||
[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:41:52 2007'' |
Revision as of 14:37, 30 October 2007
|
AMPC BETA-LACTAMASE FROM ESCHERICHIA COLI
Overview
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 Structure
2BLS is a [Single protein] structure of sequence from [Escherichia coli]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Sites: ACB and ACT. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Tue Oct 30 16:41:52 2007
