An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity

TRiC/CCT assists the folding of ∼10% of cytosolic proteins through an ATP-driven conformational cycle and is essential in maintaining protein homeostasis. Here, we determined an ensemble of cryo-electron microscopy (cryo-EM) structures of yeast TRiC at various nucleotide concentrations, with 4 open-...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2019-09, Vol.116 (39), p.19513-19522
Hauptverfasser:	Jin, Mingliang, Han, Wenyu, Liu, Caixuan, Zang, Yunxiang, Li, Jiawei, Wang, Fangfang, Wang, Yanxing, Cong, Yao
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine diphosphate Adenosine triphosphatase Adenosine Triphosphatases - metabolism Adenosine triphosphate Allosteric properties Biological Sciences Chaperonin Containing TCP-1 - metabolism Chaperonin Containing TCP-1 - physiology Chaperonin Containing TCP-1 - ultrastructure Chaperonins - metabolism Cryoelectron Microscopy - methods Electron microscopy Homeostasis Models, Molecular Molecular Conformation Nucleotides PNAS Plus Protein Folding Protein Subunits - metabolism Proteins Proteostasis Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Structure-Activity Relationship Substrate Specificity - physiology Substrates Yeast Yeasts
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