The Acylation Mechanism of CTX-M -Lactamase at 0.88 Å Resolution
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- 作者：Yu Chen ; Richard Bonnet ; Brian K. Shoichet
- 刊名：Journal of the American Chemical Society
- 出版年：2007
- 出版时间：May 2, 2007
- 年：2007
- 卷：129
- 期：17
- 页码：5378 - 5380
- 全文大小：241K
- 年卷期：v.129,no.17(May 2, 2007)
- ISSN：1520-5126
文摘
The apo crystal structure of CTX-M-9 
-lactamase has been determined to 0.88 Å at pH 8.8. This unusually clear picture of proton positions and residue interactions supports the role of Glu166 as the general base for the controversial acylation step of class A -lactamase catalysis. The ability to distinguish low-energy conformations sampled by the enzyme allows us to link the two conformations of Lys73 to different protonation states of Glu166.
-lactamase has been determined to 0.88 Å at pH 8.8. This unusually clear picture of proton positions and residue interactions supports the role of Glu166 as the general base for the controversial acylation step of class A -lactamase catalysis. The ability to distinguish low-energy conformations sampled by the enzyme allows us to link the two conformations of Lys73 to different protonation states of Glu166.