1ll5
X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem
OverviewOverview
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 StructureAbout this Structure
1LL5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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 Sat May 3 00:01:42 2008