BIROn - Birkbeck Institutional Research Online

    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.

    Full text not available from this repository.

    Abstract

    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.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): chaperones, machines, ATP driven, GroEL, Cryo-EM
    School: School of Science > Biological Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 24 Jul 2013 15:16
    Last Modified: 06 Dec 2016 11:14
    URI: https://eprints.bbk.ac.uk/id/eprint/7773

    Statistics

    Downloads
    Activity Overview
    0Downloads
    151Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item