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    A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin

    Natesh, Ramanathan and Clare, Daniel K. and Farr, G.W. and Horwich, A.L. and Saibil, Helen R. (2018) A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin. International Journal of Biological Macromolecules 118 (A), pp. 671-675. ISSN 1879-0003.

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    Abstract

    The chaperonins (GroEL and GroES in Escherichia coli) are ubiquitous molecular chaperones that assist a subset of essential substrate proteins to undergo productive folding to the native state. Using single particle cryo EM and image processing we have examined complexes of E. coli GroEL with the stringently GroE-dependent substrate enzyme RuBisCO from Rhodospirillum rubrum. Here we present snapshots of non-native RuBisCO - GroEL complexes. We observe two distinct substrate densities in the binary complex reminiscent of the two-domain structure of the RuBisCO subunit, so that this may represent a captured form of an early folding intermediate. The occupancy of the complex is consistent with the negative cooperativity of GroEL with respect to substrate binding, in accordance with earlier mass spectroscopy studies. [Abstract copyright: Copyright © 2018 The Authors. Published by Elsevier B.V. All rights reserved.]

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): Chaperonin, GroEL, Non-native protein, Protein folding, RuBisCO, Single particle cryo-EM
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    SWORD Depositor: Mr Joe Tenant
    Depositing User: Mr Joe Tenant
    Date Deposited: 24 Jul 2018 13:11
    Last Modified: 27 Jul 2019 21:35
    URI: http://eprints.bbk.ac.uk/id/eprint/23110

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