Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 116, Issue 39, Page 19513-19522, Year 2019
Publish date	Sep 24, 2019
Authors	Mingliang Jin / Wenyu Han / Caixuan Liu / Yunxiang Zang / Jiawei Li / Fangfang Wang / Yanxing Wang / Yao Cong /
PubMed Abstract	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- ...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 links	Proc Natl Acad Sci U S A / PubMed:31492816 / PubMed Central
Methods	EM (single particle)
Resolution	2.99 - 16.87 Å
Structure data	0756 6krd EMDB-0756, PDB-6krd: TRiC at 0.05 mM ADP-AlFx, Conformation 4, 0.05-C4 Method: EM (single particle) / Resolution: 4.38 Å 0757 6kre EMDB-0757, PDB-6kre: TRiC at 0.05 mM ADP-AlFx, Conformation 2, 0.05-C2 Method: EM (single particle) / Resolution: 4.45 Å 0758 6ks6 EMDB-0758, PDB-6ks6: TRiC at 0.2 mM ADP-AlFx, Conformation 1, 0.2-C1 Method: EM (single particle) / Resolution: 2.99 Å 0759 6ks7 EMDB-0759, PDB-6ks7: TRiC at 0.1 mM ADP-AlFx, Conformation 1, 0.1-C1 Method: EM (single particle) / Resolution: 4.62 Å 0760 6ks8 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: 4.0 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 moleculeYM / Adenosine diphosphate ChemComp-MG: Unknown entry ChemComp-AF3: ALUMINUM FLUORIDE / Aluminium fluoride ChemComp-HOH*: WATER / Water
Source	saccharomyces cerevisiae s288c (yeast) Saccharomyces cerevisiae (brewer's yeast)
Keywords	CHAPERONE / Chaperonin TRiC/CCT / Allosteric network / ATPase cycle / Conformational landscape / Cryo-EM