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TitleAn ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 116, Issue 39, Page 19513-19522, Year 2019
Publish dateSep 24, 2019
AuthorsMingliang Jin / Wenyu Han / Caixuan Liu / Yunxiang Zang / Jiawei Li / Fangfang Wang / Yanxing Wang / Yao Cong /
PubMed AbstractTRiC/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- ...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-state maps resolved at near-atomic resolutions, and a closed-state map at atomic resolution, revealing an extra layer of an unforeseen N-terminal allosteric network. We found that, during TRiC ring closure, the CCT7 subunit moves first, responding to nucleotide binding; CCT4 is the last to bind ATP, serving as an ATP sensor; and CCT8 remains ADP-bound and is hardly involved in the ATPase-cycle in our experimental conditions; overall, yeast TRiC consumes nucleotide in a 2-ring positively coordinated manner. Our results depict a thorough picture of the TRiC conformational landscape and its allosteric transitions from the open to closed states in more structural detail and offer insights into TRiC subunit specificity in ATP consumption and ring closure, and potentially in substrate processing.
External linksProc Natl Acad Sci U S A / PubMed:31492816 / PubMed Central
MethodsEM (single particle)
Resolution2.99 - 16.87 Å
Structure data

EMDB-0756, PDB-6krd:
TRiC at 0.05 mM ADP-AlFx, Conformation 4, 0.05-C4
Method: EM (single particle) / Resolution: 4.38 Å

EMDB-0757, PDB-6kre:
TRiC at 0.05 mM ADP-AlFx, Conformation 2, 0.05-C2
Method: EM (single particle) / Resolution: 4.45 Å

EMDB-0758, PDB-6ks6:
TRiC at 0.2 mM ADP-AlFx, Conformation 1, 0.2-C1
Method: EM (single particle) / Resolution: 2.99 Å

EMDB-0759, PDB-6ks7:
TRiC at 0.1 mM ADP-AlFx, Conformation 1, 0.1-C1
Method: EM (single particle) / Resolution: 4.62 Å

EMDB-0760, PDB-6ks8:
TRiC at 0.1 mM ADP-AlFx, Conformation 4, 0.1-C4
Method: EM (single particle) / Resolution: 4.69 Å

EMDB-0761:
TRiC at 0.1 mM ADP-AlFx, Conformation 2a, 0.1-C2a
Method: EM (single particle) / Resolution: 12.98 Å

EMDB-0762:
TRiC at 0.1 mM ADP-AlFx, Conformation 2b, 0.1-C2b
Method: EM (single particle) / Resolution: 7.67 Å

EMDB-0763:
TRiC at 0.1 mM ADP-AlFx, Conformation 3, 0.1-C3
Method: EM (single particle) / Resolution: 16.87 Å

EMDB-0764:
TRiC at 0.05 mM ADP-AlFx, Conformation 1, 0.05-C1
Method: EM (single particle) / Resolution: 6.8 Å

EMDB-0765:
TRiC at 0.05 mM ADP-AlFx, Conformation 3, 0.05-C3
Method: EM (single particle) / Resolution: 7.18 Å

EMDB-0766:
TRiC at 0.2 mM ATP, 0.2-ATP
Method: EM (single particle) / Resolution: 4 Å

EMDB-0767:
TRiC at 0.5 mM ADP-AlFx, Conformation 1, 0.5-C1
Method: EM (single particle) / Resolution: 3.44 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-MG:
MAGNESIUM ION / Magnesium

ChemComp-AF3:
ALUMINUM FLUORIDE / Aluminium fluoride

ChemComp-HOH:
WATER / Water

Source
  • saccharomyces cerevisiae s288c (yeast)
  • Baker's yeast (baker's yeast)
  • Saccharomyces cerevisiae (baker's yeast)
KeywordsAdenosine Triphosphatases / CCT4 protein, S cerevisiae / Chaperonin Containing TCP-1 / Chaperonins / Cryoelectron Microscopy / Models, Molecular / Molecular Conformation / Protein Folding / Protein Subunits / Proteostasis / Saccharomyces cerevisiae / Saccharomyces cerevisiae Proteins / Structure-Activity Relationship / Substrate Specificity / CHAPERONE / Chaperonin TRiC/CCT / Allosteric network / ATPase cycle / Conformational landscape / Cryo-EM

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