Structural highlights
Function
AMPC_ECOLI This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Beadle BM, Shoichet BK. Structural basis for imipenem inhibition of class C beta-lactamases. Antimicrob Agents Chemother. 2002 Dec;46(12):3978-80. PMID:12435704
