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Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution

Nature Structural Biology volume 2, pages 1083–1094 (1995)Cite this article

Abstract

Improved refinement of the crystal structure of GroEL from Escherichia coli has resulted in a complete atomic model for the first 524 residues. A new torsion-angle dynamics method and non-crystallographic symmetry restraints were used in the refinement. The model indicates that conformational variability exists due to rigid-body movements between the apical and intermediate domains of GroEL, resulting in deviations from strict seven-fold symmetry. The regions of the protein involved in polypeptide and GroES binding show unusually high B factors; these values may indicate mobility or discrete disorder. The variability of these regions may play a role in the ability of GroEL to bind a wide variety of substrates.

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Author notes

  1. Kerstin Braig

    Present address: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB9 2QH, UK

Authors and Affiliations

  1. Department of Genetics, Yale University, New Haven, Connecticut, 06510, USA

    Kerstin Braig

  2. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, 06520, USA

    Paul D. Adams

  3. The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, 06520, USA

    Axel T. Brünger

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  2. Paul D. Adams
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  3. Axel T. Brünger
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Braig, K., Adams, P. & Brünger, A. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nat Struct Mol Biol 2, 1083–1094 (1995). https://doi.org/10.1038/nsb1295-1083

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