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| | <SX load='6ks8' size='340' side='right' viewer='molstar' caption='[[6ks8]], [[Resolution|resolution]] 4.69Å' scene=''> | | <SX load='6ks8' size='340' side='right' viewer='molstar' caption='[[6ks8]], [[Resolution|resolution]] 4.69Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ks8]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KS8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KS8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ks8]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KS8 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ks8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks8 OCA], [http://pdbe.org/6ks8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ks8 RCSB], [http://www.ebi.ac.uk/pdbsum/6ks8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks8 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.69Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ks8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks8 OCA], [https://pdbe.org/6ks8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ks8 RCSB], [https://www.ebi.ac.uk/pdbsum/6ks8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TCPH_YEAST TCPH_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity). [[http://www.uniprot.org/uniprot/TCPD_YEAST TCPD_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPQ_YEAST TCPQ_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity). [[http://www.uniprot.org/uniprot/TCPB_YEAST TCPB_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPZ_YEAST TCPZ_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPA_YEAST TCPA_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPE_YEAST TCPE_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPG_YEAST TCPG_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. | + | [https://www.uniprot.org/uniprot/TCPA_YEAST TCPA_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6ks8" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ks8" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Chaperonin 3D structures|Chaperonin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Saccharomyces cerevisiae s288c]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Cong, Y]] | + | [[Category: Cong Y]] |
| - | [[Category: Jin, M]] | + | [[Category: Jin M]] |
| - | [[Category: Allosteric network]]
| + | |
| - | [[Category: Atpase cycle]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Chaperonin tric/cct]]
| + | |
| - | [[Category: Conformational landscape]]
| + | |
| - | [[Category: Cryo-em]]
| + | |
| Structural highlights
Function
TCPA_YEAST Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
Publication Abstract from PubMed
TRiC/CCT assists the folding of approximately 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.
An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.,Jin M, Han W, Liu C, Zang Y, Li J, Wang F, Wang Y, Cong Y Proc Natl Acad Sci U S A. 2019 Sep 24;116(39):19513-19522. doi:, 10.1073/pnas.1903976116. Epub 2019 Sep 6. PMID:31492816[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jin M, Han W, Liu C, Zang Y, Li J, Wang F, Wang Y, Cong Y. An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity. Proc Natl Acad Sci U S A. 2019 Sep 24;116(39):19513-19522. doi:, 10.1073/pnas.1903976116. Epub 2019 Sep 6. PMID:31492816 doi:http://dx.doi.org/10.1073/pnas.1903976116
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