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	Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.
Journal, issue, pages	EMBO J, Vol. 31, Issue 3, Page 720-730, Year 2012
Publish date	Feb 1, 2012
Authors	Yao Cong / Gunnar F Schröder / Anne S Meyer / Joanita Jakana / Boxue Ma / Matthew T Dougherty / Michael F Schmid / Stefanie Reissmann / Michael Levitt / Steven L Ludtke / Judith Frydman / Wah Chiu /
PubMed Abstract	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 ...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 without imposing symmetry during the 3D reconstruction. These structures reveal the intra- and inter-ring subunit interaction pattern changes during the ATPase cycle. In the apo state, the subunit arrangement in each ring is highly asymmetric, whereas all nucleotide-containing states tend to be more symmetrical. We identify and structurally characterize an one-ring closed intermediate induced by ATP hydrolysis wherein the closed TRiC ring exhibits an observable chamber expansion. This likely represents the physiological substrate folding state. Our structural results suggest mechanisms for inter-ring-negative cooperativity, intra-ring-positive cooperativity, and protein-folding chamber closure of TRiC. Intriguingly, these mechanisms are different from other group I and II chaperonins despite their similar architecture.
External links	EMBO J / PubMed:22045336 / PubMed Central
Methods	EM (single particle)
Resolution	10.5 - 13.9 Å
Structure data	1960 4a0o EMDB-1960, PDB-4a0o: Symmetry-free cryo-EM map of TRiC in the nucleotide-free (apo) state Method: EM (single particle) / Resolution: 10.5 Å 1961 4a0v EMDB-1961: Symmetry-free cryo-EM map of TRiC-AMP-PNP PDB-4a0v: model refined against the Symmetry-free cryo-EM map of TRiC-AMP-PNP Method: EM (single particle) / Resolution: 10.7 Å 1962 4a0w EMDB-1962: Symmetry-free cryo-EM map of TRiC-ADP-AlFx PDB-4a0w: model built against symmetry-free cryo-EM map of TRiC-ADP-AlFx Method: EM (single particle) / Resolution: 13.9 Å 1963 4a13 EMDB-1963: Symmetry-free cryo-EM map of TRiC-ADP PDB-4a13: model refined against symmetry-free cryo-EM map of TRiC-ADP Method: EM (single particle) / Resolution: 11.3 Å
Source	bos taurus (cattle)
Keywords	CHAPERONE / CHAPERONIN / PROTEIN FOLDING