Structural basis for imipenem inhibition of class C β-lactamases

被引:64
作者
Beadle, BM [1 ]
Shoichet, BK [1 ]
机构
[1] Northwestern Univ, Dept Mol Pharmacol & Biol Chem, Chicago, IL 60611 USA
关键词
D O I
10.1128/AAC.46.12.3978-3980.2002
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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 Angstrom. In the complex, the lactam carbonyl oxygen of imipenem has flipped by approximately 180degrees 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.
引用
收藏
页码:3978 / 3980
页数:3
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