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

The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar subunits arranged in two stacked rings. Substrate folding inside the central chamber is triggered by ATP hydrolysis. We present five cryo-EM structures of TRiC in apo and nucleotide-induced states wit...

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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
Formato: Artigo
Idioma:Inglês
Publicado: Nature Publishing Group 2012
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC3273382/
https://ncbi.nlm.nih.gov/pubmed/22045336
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/emboj.2011.366
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