1ll5
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1ll5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ll5, resolution 1.80Å" /> '''X-ray crystal struct...)
Next diff →
Revision as of 18:31, 20 November 2007
|
X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem
Overview
To determine how imipenem inhibits the class C beta-lactamase AmpC, the, X-ray crystal structure of the acyl-enzyme complex was determined to a, resolution of 1.80 A. In the complex, the lactam carbonyl oxygen of, imipenem has flipped by approximately 180 degrees compared to its expected, position; the electrophilic acyl center is thus displaced from the point, of hydrolytic attack. This conformation resembles that of imipenem bound, to the class A enzyme TEM-1 but is different from that of moxalactam bound, to AmpC.
About this Structure
1LL5 is a Single protein structure of sequence from Escherichia coli with IM2 as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
Structural basis for imipenem inhibition of class C beta-lactamases., Beadle BM, Shoichet BK, Antimicrob Agents Chemother. 2002 Dec;46(12):3978-80. PMID:12435704
Page seeded by OCA on Tue Nov 20 20:38:45 2007
