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Structural basis for imipenem inhibition of class C beta-lactamases ANTIMICROBIAL AGENTS AND CHEMOTHERAPY Beadle, B. M., Shoichet, B. K. 2002; 46 (12): 3978-3980

Abstract

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.

View details for DOI 10.1128/AAC.46.12.3978-3980.2002

View details for Web of Science ID 000179376000041

View details for PubMedID 12435704

View details for PubMedCentralID PMC132770