期刊
BIOCHEMISTRY
卷 46, 期 14, 页码 4370-4378出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi602335x
关键词
-
资金
- NCI NIH HHS [CA69202] Funding Source: Medline
- NIBIB NIH HHS [EB01958, R01 EB001958] Funding Source: Medline
- NIGMS NIH HHS [P01 GM068036, 5P01GM068036] Funding Source: Medline
The Yersinia protein tyrosine phosphatase (YopH) contains a loop of ten amino acids (the WPD loop) that covers the entrance of the active site of the enzyme during substrate binding. In this work the substrate mimicking competitive inhibitor p-nitrocatechol sulfate (PNC) is used as a probe of the active site. The dynamics of the WPD loop was determined by subjecting an equilibrated system containing YopH, PNC, and YopH bound to PNC to a laser induced temperature jump, and subsequently following the change in equilibrium due to the perturbation. Using this methodology the dynamics associated with substrate binding in YopH have been determined. These results indicate that substrate binding is coupled to the WPD loop motion, and WPD loop dynamics occur in the sub-millisecond time scale. The significance of these dynamic results is interpreted in terms of the catalytic cycle of the enzyme.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据