8sgq: Difference between revisions
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The | ==CCT G beta 5 complex intermediate state== | ||
<StructureSection load='8sgq' size='340' side='right'caption='[[8sgq]], [[Resolution|resolution]] 3.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8sgq]] is a 16 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=8SGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SGQ 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]] 3.7Å</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=8sgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sgq OCA], [https://pdbe.org/8sgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sgq RCSB], [https://www.ebi.ac.uk/pdbsum/8sgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sgq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TCPB_HUMAN TCPB_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 == | |||
The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with beta-propeller domains. Here, we determine the structures of human CCT in complex with its accessory co-chaperone, phosducin-like protein 1 (PhLP1), in the process of folding Gbeta(5), a component of Regulator of G protein Signaling (RGS) complexes. Cryoelectron microscopy (cryo-EM) and image processing reveal an ensemble of distinct snapshots that represent the folding trajectory of Gbeta(5) from an unfolded molten globule to a fully folded beta-propeller. These structures reveal the mechanism by which CCT directs Gbeta(5) folding through initiating specific intermolecular contacts that facilitate the sequential folding of individual beta sheets until the propeller closes into its native structure. This work directly visualizes chaperone-mediated protein folding and establishes that CCT orchestrates folding by stabilizing intermediates through interactions with surface residues that permit the hydrophobic core to coalesce into its folded state. | |||
Visualizing the chaperone-mediated folding trajectory of the G protein beta5 beta-propeller.,Wang S, Sass MI, Kwon Y, Ludlam WG, Smith TM, Carter EJ, Gladden NE, Riggi M, Iwasa JH, Willardson BM, Shen PS Mol Cell. 2023 Oct 11:S1097-2765(23)00795-5. doi: 10.1016/j.molcel.2023.09.032. PMID:37852256<ref>PMID:37852256</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8sgq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Sass M]] | |||
[[Category: Shen PS]] | |||
[[Category: Wang S]] | |||
[[Category: Willardson BM]] | |||
Revision as of 16:14, 1 November 2023
CCT G beta 5 complex intermediate stateCCT G beta 5 complex intermediate state
Structural highlights
FunctionTCPB_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).[1] [2] Publication Abstract from PubMedThe Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with beta-propeller domains. Here, we determine the structures of human CCT in complex with its accessory co-chaperone, phosducin-like protein 1 (PhLP1), in the process of folding Gbeta(5), a component of Regulator of G protein Signaling (RGS) complexes. Cryoelectron microscopy (cryo-EM) and image processing reveal an ensemble of distinct snapshots that represent the folding trajectory of Gbeta(5) from an unfolded molten globule to a fully folded beta-propeller. These structures reveal the mechanism by which CCT directs Gbeta(5) folding through initiating specific intermolecular contacts that facilitate the sequential folding of individual beta sheets until the propeller closes into its native structure. This work directly visualizes chaperone-mediated protein folding and establishes that CCT orchestrates folding by stabilizing intermediates through interactions with surface residues that permit the hydrophobic core to coalesce into its folded state. Visualizing the chaperone-mediated folding trajectory of the G protein beta5 beta-propeller.,Wang S, Sass MI, Kwon Y, Ludlam WG, Smith TM, Carter EJ, Gladden NE, Riggi M, Iwasa JH, Willardson BM, Shen PS Mol Cell. 2023 Oct 11:S1097-2765(23)00795-5. doi: 10.1016/j.molcel.2023.09.032. PMID:37852256[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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