由ATP触发的形状变化划分了GroEL chaperonin的基质结合和折叠机制
Daniel K Clare1, Daven Vasishtan, Scott Stagg
1Crystallography and Institute of Structural and Molecular Biology, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK.
Cell
|March 27, 2012
概括
沙佩罗宁GroEL蛋白与CochaperoninGroES一起使用ATP封装和折叠蛋白质. 显而易见的GroEL-ATP形状揭示了将错误折叠的基板喷射到水友室的机械过程.
科学领域:
- 分子生物学分子生物学
- 结构生物学是结构生物学.
- 生物化学 生物化学
背景情况:
- 像GroEL这样的Chaperonin对于蛋白质折叠至关重要.
- GroEL促进新生或变质的多的折叠.
- ATP结合和cochaperonin GroES对于GroEL功能至关重要.
研究的目的:
- 为了解决不同的GroEL-ATP形状.
- 了解GroEL的蛋白质折叠和喷射的机械机制.
- 阐明域移动在基质捕获和释放中的作用.
主要方法:
- 低温电子显微镜的使用方法
- 统计分析 统计分析
- 灵活的装配技术可以提供灵活的装配技术.
主要成果:
- 确定了GroEL-ATP形状的轨迹,显示域旋转和升高.
- 最初的形状捕获了多基质.
- 延伸的形状施加机械力,并促进GroES结合用于基板喷射.
结论:
- GroEL-ATP构造定义了蛋白质折叠的机械路径.
- 域移动对于基质结合,操纵和释放至关重要.
- GroEL-GroES-ATP系统为细胞蛋白质平衡提供了一个强大的机制.
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