The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL

Alan M. Roseman, Shaoxia Chen, Helen White, Kerstin Braig, Helen R. Saibil

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by the large chaperonin GroEL, which undergoes major allosteric rearrangements. Interaction between the two back-to-back seven- membered rings of GroEL plays an important role in regulating binding and release of folding substrates and of the small chaperonin GroES. Using cryo- electron microscopy, we have obtained three-dimensional reconstructions to 30 Å resolution for GroEL and GroEL-GroES complexes in the presence of ADP, ATP, and the nonhydrolyzable ATP analog, AMP-PNP. Nucleotide binding to the equatorial domains of GroEL causes large rotations of the apical domains, containing the GroES and substrate protein-binding sites. We propose a mechanism for allosteric switching and describe conformational changes that may be involved in critical steps of folding for substrates encapsulated by GroES.
    Original languageEnglish
    Pages (from-to)241-251
    Number of pages10
    JournalCell
    Volume87
    Issue number2
    DOIs
    Publication statusPublished - 18 Oct 1996

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