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

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

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...

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Bibliographic Details
Main Authors: Cong, Yao, Schröder, Gunnar F, Meyer, Anne S, Jakana, Joanita, Ma, Boxue, Dougherty, Matthew T, Schmid, Michael F, Reissmann, Stefanie, Levitt, Michael, Ludtke, Steven L, Frydman, Judith, Chiu, Wah
Format: Online
Language:English
Published: Nature Publishing Group 2012
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3273382/

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https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3273382/

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