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Mechanism of folding chamber closure in a group II chaperonin

Author

Listed:
  • Junjie Zhang

    (Graduate Program in Structural and Computational Biology and Molecular Biophysics,
    National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA)

  • Matthew L. Baker

    (National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA)

  • Gunnar F. Schröder

    (Department of Structural Biology,
    Present addresses: Institut für Strukturbiologie und Biophysik (ISB-3), Forschungszentrum Jülich, 52425 Jülich, Germany (G.F.S.); Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch Strasse, 35043 Marburg, Germany (S.R.).)

  • Nicholai R. Douglas

    (Stanford University, Stanford, California 94305, USA)

  • Stefanie Reissmann

    (Stanford University, Stanford, California 94305, USA
    Present addresses: Institut für Strukturbiologie und Biophysik (ISB-3), Forschungszentrum Jülich, 52425 Jülich, Germany (G.F.S.); Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch Strasse, 35043 Marburg, Germany (S.R.).)

  • Joanita Jakana

    (National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA)

  • Matthew Dougherty

    (National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA)

  • Caroline J. Fu

    (National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA)

  • Michael Levitt

    (Department of Structural Biology,)

  • Steven J. Ludtke

    (Graduate Program in Structural and Computational Biology and Molecular Biophysics,
    National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA)

  • Judith Frydman

    (Stanford University, Stanford, California 94305, USA)

  • Wah Chiu

    (Graduate Program in Structural and Computational Biology and Molecular Biophysics,
    National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA)

Abstract

Folding cycles in group II chaperonins Chaperonins are large, cylindrical complexes that assist in the folding of cellular proteins in an ATP-dependent manner. Group II chaperonins are present in eukaryotes and archaea and consist of two back-to-back rings and a lid segment extending from an apical domain. In this study, Wah Chiu and colleagues determine the cryo-electron microscopy structure of an archael chaperonin called Mm-cpn in the nucleotide-free (open) and nucleotide-induced (closed) states. The structure provides details on conformational changes triggered by ATP hydrolysis leading to rearrangements in inter-ring subunits that differ from other classes of chaperonins.

Suggested Citation

  • Junjie Zhang & Matthew L. Baker & Gunnar F. Schröder & Nicholai R. Douglas & Stefanie Reissmann & Joanita Jakana & Matthew Dougherty & Caroline J. Fu & Michael Levitt & Steven J. Ludtke & Judith Frydm, 2010. "Mechanism of folding chamber closure in a group II chaperonin," Nature, Nature, vol. 463(7279), pages 379-383, January.
    • Handle: RePEc:nat:nature:v:463:y:2010:i:7279:d:10.1038_nature08701
    DOI: 10.1038/nature08701
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