View source for 7wu7


==Prefoldin-tubulin-TRiC complex==
<StructureSection load='7wu7' size='340' side='right'caption='[[7wu7]], [[Resolution|resolution]] 3.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wu7]] is a 14 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=7WU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WU7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></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=7wu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wu7 OCA], [https://pdbe.org/7wu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wu7 RCSB], [https://www.ebi.ac.uk/pdbsum/7wu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wu7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PFD1_HUMAN PFD1_HUMAN] Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis. To uncover why some eukaryotic proteins can only fold with TRiC assistance, we reconstituted the folding of beta-tubulin using human prefoldin and TRiC. We find unstructured beta-tubulin is delivered by prefoldin to the open TRiC chamber followed by ATP-dependent chamber closure. Cryo-EM resolves four near-atomic-resolution structures containing progressively folded beta-tubulin intermediates within the closed TRiC chamber, culminating in native tubulin. This substrate folding pathway appears closely guided by site-specific interactions with conserved regions in the TRiC chamber. Initial electrostatic interactions between the TRiC interior wall and both the folded tubulin N domain and its C-terminal E-hook tail establish the native substrate topology, thus enabling C-domain folding. Intrinsically disordered CCT C termini within the chamber promote subsequent folding of tubulin's core and middle domains and GTP-binding. Thus, TRiC's chamber provides chemical and topological directives that shape the folding landscape of its obligate substrates.

Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.,Gestaut D, Zhao Y, Park J, Ma B, Leitner A, Collier M, Pintilie G, Roh SH, Chiu W, Frydman J Cell. 2022 Dec 8;185(25):4770-4787.e20. doi: 10.1016/j.cell.2022.11.014. PMID:36493755<ref>PMID:36493755</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wu7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chiu W]]
[[Category: Collier M]]
[[Category: Frydman J]]
[[Category: Gestaut D]]
[[Category: Leitner A]]
[[Category: Ma B]]
[[Category: Park J]]
[[Category: Pintilie G]]
[[Category: Roh S-H]]
[[Category: Zhao Y]]