Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle

• Yao Cong ^[1] ; Gunnar F Schröder ^[2] ; Anne S Meyer ^[2] ; Joanita Jakana ^[1] ; Boxue Ma ^[1] ; Matthew T Dougherty ^[1] ; Michael F Schmid ^[1] ; Stefanie Reissmann ^[2] ; Michael Levitt ^[2] ; Steven L Ludtke ^[1] ; Judith Frydman ^[2] ; Wah Chiu ^[1]
  1. [1] Baylor College of Medicine

     Baylor College of Medicine

     Estados Unidos

     
  2. [2] Stanford University

     Stanford University

     Estados Unidos

     
• Localización: EMBO journal: European Molecular Biology Organization, ISSN 0261-4189, Vol. 31, Nº. 3, 2011, págs. 720-730
• Idioma: inglés
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• Resumen

  • Chaperonins are multisubunit entities that are composed of two stacked rings enclosing a central chamber for ATP-dependent protein folding. A series of cryo-EM structures of the eukaryotic group II chaperonin TRiC/CCT reveal the conformational changes during the ATPase cycle and provide insight into how the subunits cooperate to close the lid.