一个域间的能量拉战,在Hsp70分子伴侣中创造了全osterically活跃的状态
Anastasia Zhuravleva1, Eugenia M Clerico, Lila M Gierasch
1Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA.
Cell
|December 11, 2012
概括
热冲击蛋白70 (Hsp70) 分子陪伴者使用全ostery来调节蛋白质的结合和功能. 研究人员确定了大肠杆菌DnaK的全性活性状态,揭示了信号传输的关键相互作用.
科学领域:
- 分子生物学分子生物学
- 生物化学 生物化学
- 结构生物学是结构生物学.
背景情况:
- Hsp70分子陪伴者通过依赖ATP的全性机制调节蛋白质平衡.
- 体调节涉及核酸结合域 (NBD) 和基质结合域 (SBD) 之间的通信.
- Hsp70s循环通过不同的状态,包括对功能至关重要的"全质活性"状态.
研究的目的:
- 为了捕捉和描述大肠杆菌Hsp70的全性活性状态,DnaK.
- 阐明在Hsp70.0.内调解全信号传输的分子相互作用.
主要方法:
- 生物化学捕获全性活性状态.
- 蛋白质 - 配体相互作用的结构分析.
- 研究域间通信通道的研究.
主要成果:
- DnaK的全性活性状态被成功捕获.
- 在NBD,SBD β子域,SBD α-螺旋盖和域间链接器之间确定了关键相互作用.
- 阿洛斯特信号传输是由域形态和特定接口之间的能量平衡驱动的.
结论:
- 这项研究揭示了Hsp70全菌的结构基础.
- 了解这些机制,可以深入了解Hsp70的功能调节由连接体和cochaperones.
- 这项工作有助于了解Hsp70s是如何在进化过程中调整到功能上的.
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