GroEL-GroES循环:ATP和非原生多直接交替的折叠活性环
1Howard Hughes Medical Institute, and Department of Genetics, Yale School of Medicine, New Haven, Connecticut 06510, USA.
Cell
|May 13, 1999
概括
司机GroEL使用ATP水解来替代蛋白质折叠环. 这一循环确保了高效的蛋白质重折叠,通过在GroES之前结合非原生多,优化伴奏蛋白.
科学领域:
- 分子生物学分子生物学
- 蛋白质的生物化学 蛋白质的生物化学
- 蜂机械 蜂机械 蜂机械
背景情况:
- 双环护卫剂GroEL促进了其中心腔内的蛋白质折叠.
- 这一过程涉及结合ATP和GroES的cochaperonin.
- 在折叠活跃状态之间的GroEL功能循环的精确机制仍然不完全理解.
研究的目的:
- 阐明了指导人格GroEL的功能循环的序列事件.
- 为了确定基质和cochaperonin结合的顺序相对于ATP水解和环形状变化.
- 了解GroEL如何在连续的蛋白质折叠周期之间过渡.
主要方法:
- 生物化学分析监测ATP水解速率.
- 分析聚和GroES结合动力学.
- 在GroEL的角域中观察形状变化.
主要成果:
- 在cis环中的ATP水解是非原生多或GroES与转环结合的先决条件.
- 这种水解事件伴随着转环的顶端域的重定位.
- 对新开放的转环的聚结合刺激了现有的cis复合物的解离,促进了GroES结合和随后的折叠.
结论:
- GroEL的功能周期涉及一个严格的事件顺序:ATP水解,多结合和GroES结合.
- 沙佩罗宁交替其两个环,每个环连续作为一个折叠活跃的cis复合体.
- 这种交替机制允许高效的蛋白质折叠,在非原生蛋白质的存在下,每次折叠事件只使用一个七个ATP的循环.
更多相关视频
10:31Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
Published on: February 3, 2022
10:19Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin
Published on: January 24, 2025
相关概念视频
01:22Protein Folding
Overview
01:22Protein Folding
Overview
03:00Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
01:48ATP Synthase: Mechanism
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
01:25Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
03:00Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...