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	Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.
Journal, issue, pages	Commun Biol, Vol. 6, Issue 1, Page 531, Year 2023
Publish date	May 16, 2023
Authors	Caixuan Liu / Mingliang Jin / Shutian Wang / Wenyu Han / Qiaoyu Zhao / Yifan Wang / Cong Xu / Lei Diao / Yue Yin / Chao Peng / Lan Bao / Yanxing Wang / Yao Cong /
PubMed Abstract	The eukaryotic chaperonin TRiC/CCT assists the folding of about 10% of cytosolic proteins through an ATP-driven conformational cycle, and the essential cytoskeleton protein tubulin is the obligate ...The eukaryotic chaperonin TRiC/CCT assists the folding of about 10% of cytosolic proteins through an ATP-driven conformational cycle, and the essential cytoskeleton protein tubulin is the obligate substrate of TRiC. Here, we present an ensemble of cryo-EM structures of endogenous human TRiC throughout its ATPase cycle, with three of them revealing endogenously engaged tubulin in different folding stages. The open-state TRiC-tubulin-S1 and -S2 maps show extra density corresponding to tubulin in the cis-ring chamber of TRiC. Our structural and XL-MS analyses suggest a gradual upward translocation and stabilization of tubulin within the TRiC chamber accompanying TRiC ring closure. In the closed TRiC-tubulin-S3 map, we capture a near-natively folded tubulin-with the tubulin engaging through its N and C domains mainly with the A and I domains of the CCT3/6/8 subunits through electrostatic and hydrophilic interactions. Moreover, we also show the potential role of TRiC C-terminal tails in substrate stabilization and folding. Our study delineates the pathway and molecular mechanism of TRiC-mediated folding of tubulin along the ATPase cycle of TRiC, and may also inform the design of therapeutic agents targeting TRiC-tubulin interactions.
External links	Commun Biol / PubMed:37193829 / PubMed Central
Methods	EM (single particle)
Resolution	3.1 - 4.5 Å
Structure data	32903 7wz3 EMDB-32903, PDB-7wz3: Cryo-EM structure of human TRiC-tubulin-S1 state Method: EM (single particle) / Resolution: 4.1 Å 32922 7x0a EMDB-32922, PDB-7x0a: Cryo-EM structure of human TRiC-NPP state Method: EM (single particle) / Resolution: 3.1 Å 32923 7x0s EMDB-32923, PDB-7x0s: Human TRiC-tubulin-S3 Method: EM (single particle) / Resolution: 3.1 Å 32926 7x0v EMDB-32926, PDB-7x0v: cryo-EM structure of human TRiC-ADP-AlFx Method: EM (single particle) / Resolution: 3.2 Å 32989 7x3j EMDB-32989, PDB-7x3j: Cryo-EM structure of human TRiC-tubulin-S2 Method: EM (single particle) / Resolution: 4.2 Å 32993 7x3u EMDB-32993, PDB-7x3u: cryo-EM structure of human TRiC-ADP Method: EM (single particle) / Resolution: 3.3 Å 33025 7x6q EMDB-33025, PDB-7x6q: cryo-EM structure of human TRiC-ATP-closed state Method: EM (single particle) / Resolution: 4.5 Å 33053 7x7y EMDB-33053, PDB-7x7y: Cryo-EM structure of Human TRiC-ATP-open state Method: EM (single particle) / Resolution: 3.8 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 ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate
Source	homo sapiens (human)
Keywords	STRUCTURAL PROTEIN / tubulin / Human TRiC