由三磷酸腺苷驱动的分子伴侣机器。

Clare Daniel K, Saibil Helen R

Department of Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK.

Biopolymers. 2013 Nov;99(11):846-59. doi: 10.1002/bip.22361.

This review is focused on the mechanisms by which ATP binding and hydrolysis drive chaperone machines assisting protein folding and unfolding. A survey of the key, general chaperone systems Hsp70 and Hsp90, and the unfoldase Hsp100 is followed by a focus on the Hsp60 chaperonin machine which is understood in most detail. Cryo-electron microscopy analysis of the E. coli Hsp60 GroEL reveals intermediate conformations in the ATPase cycle and in substrate folding. These structures suggest a mechanism by which GroEL can forcefully unfold and then encapsulate substrates for subsequent folding in isolation from all other binding surfaces.

本综述聚焦于ATP结合与水解驱动伴侣机器协助蛋白质折叠与去折叠的机制。在概述关键的通用伴侣系统Hsp70和Hsp90以及解折叠酶Hsp100之后，重点关注了解最为详细的Hsp60伴侣蛋白机器。对大肠杆菌Hsp60 GroEL的冷冻电子显微镜分析揭示了ATP酶循环和底物折叠过程中的中间构象。这些结构提示了一种机制，通过该机制GroEL能够强力展开底物，然后将其包裹起来，以便后续在与所有其他结合表面隔离的情况下进行折叠。