View source for 6nrb


==hTRiC-hPFD Class2==
<SX load='6nrb' size='340' side='right' viewer='molstar' caption='[[6nrb]], [[Resolution|resolution]] 8.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nrb]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NRB 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]] 8.7&#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=6nrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nrb OCA], [https://pdbe.org/6nrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nrb RCSB], [https://www.ebi.ac.uk/pdbsum/6nrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nrb ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/TCPA_HUMAN TCPA_HUMAN] Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:20080638</ref> <ref>PMID:25467444</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Maintaining proteostasis in eukaryotic protein folding involves cooperation of distinct chaperone systems. To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the chaperone prefoldin/GIMc (PFD), we integrate cryoelectron microscopy (cryo-EM), crosslinking-mass-spectrometry and biochemical and cellular approaches to elucidate the structural and functional interplay between TRiC/CCT and PFD. We find these hetero-oligomeric chaperones associate in a defined architecture, through a conserved interface of electrostatic contacts that serves as a pivot point for a TRiC-PFD conformational cycle. PFD alternates between an open "latched" conformation and a closed "engaged" conformation that aligns the PFD-TRiC substrate binding chambers. PFD can act after TRiC bound its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles. Disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates. The supra-chaperone assembly formed by PFD and TRiC is essential to prevent toxic conformations and ensure effective cellular proteostasis.

The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis.,Gestaut D, Roh SH, Ma B, Pintilie G, Joachimiak LA, Leitner A, Walzthoeni T, Aebersold R, Chiu W, Frydman J Cell. 2019 Apr 18;177(3):751-765.e15. doi: 10.1016/j.cell.2019.03.012. Epub 2019 , Apr 4. PMID:30955883<ref>PMID:30955883</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 6nrb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
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</SX>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Aebersold R]]
[[Category: Chiu W]]
[[Category: Frydman J]]
[[Category: Gestaut DR]]
[[Category: Joachimiak LA]]
[[Category: Leitner A]]
[[Category: Ma B]]
[[Category: Pintilie G]]
[[Category: Roh SH]]
[[Category: Walzthoeni T]]