Solution structure of the bacterial chemotaxis adaptor protein CheW from Escherichia coli
- 影响因子：
0.0
- 发表刊物：
Biochem. Biophys. Res. Commun
- 摘要：
The bacterial chemotaxis adaptor protein CheW physically links the chemoreceptors (MCPs) and the histidine kinase CheA. Extensive investigations using bacterium Escherichia coli have established the central role of CheW in the MCP-modulated activation of CheA. Here we report the solution structure of CheW from E. coli determined by NMR spectroscopy. The results show that E. coli CheW shares an overall fold with previously reported structure of CheW from Thermotoga maritima, whereas local conformational deviations are observed. In particular, the C-terminal alpha-helix is considerably longer in E. coli CheW and appears to shrink the active binding pocket with CheA. Our study provides the structural basis for further investigations in E. coli chemotaxis.
- 论文类型：
期刊论文
- 论文编号：
15
- 卷号：
360
- 期号：
4
- 页面范围：
863-867
- 是否译文：
否
- 发表时间：
2007-01-01
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Li You
- 通讯作者：
Jin Changwen
- 全部作者：
Hu Yunfei,Fu Wenyu,Xia Bin
