Mechanism of folding chamber closure in a group II chaperonin

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 Frydman () and Wah Chiu ()
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Junjie Zhang: Graduate Program in Structural and Computational Biology and Molecular Biophysics,
Matthew L. Baker: National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, Texas 77030, USA
Gunnar F. Schröder: Department of Structural Biology,
Nicholai R. Douglas: Stanford University, Stanford, California 94305, USA
Stefanie Reissmann: Stanford University, Stanford, California 94305, USA
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,
Judith Frydman: Stanford University, Stanford, California 94305, USA
Wah Chiu: Graduate Program in Structural and Computational Biology and Molecular Biophysics,

Nature, 2010, vol. 463, issue 7279, 379-383

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.

Date: 2010
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DOI: 10.1038/nature08701

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