View source for 6kre


==TRiC at 0.05 mM ADP-AlFx, Conformation 2, 0.05-C2==
<SX load='6kre' size='340' side='right' viewer='molstar' caption='[[6kre]], [[Resolution|resolution]] 4.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kre]] 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=6KRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KRE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.45&#8491;</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=6kre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kre OCA], [https://pdbe.org/6kre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kre RCSB], [https://www.ebi.ac.uk/pdbsum/6kre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kre ProSAT]</span></td></tr>
</table>
== Function ==
[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.
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== 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<ref>PMID:31492816</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6kre" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Cong Y]]
[[Category: Jin M]]