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

Yao Cong, Gunnar Schröder, Anne S. Meyer, Joanita Jakana, Boxue Ma, Matthew T. Dougherty, Michael F. Schmid, Stefanie Reissmann, Michael Levitt, Steven L Ludtke, Judith Frydman, Wah Chiu

• 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.