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    ATP-driven molecular chaperone machines

    Clare, Daniel K. and Saibil, Helen R. (2013) ATP-driven molecular chaperone machines. Biopolymers 99 (11), pp. 846-859. ISSN 0006-3525.

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    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.


    Item Type: Article
    Keyword(s) / Subject(s): chaperones, machines, ATP driven, GroEL, Cryo-EM
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 24 Jul 2013 15:16
    Last Modified: 02 Aug 2023 17:06


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