6nra
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==hTRiC-hPFD Class1 (No PFD)== | |
| + | <StructureSection load='6nra' size='340' side='right'caption='[[6nra]], [[Resolution|resolution]] 7.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6nra]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NRA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NRA FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6nra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nra OCA], [http://pdbe.org/6nra PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nra RCSB], [http://www.ebi.ac.uk/pdbsum/6nra PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nra ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/TCPE_HUMAN TCPE_HUMAN]] Hereditary sensory and autonomic neuropathy with spastic paraplegia. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TCPZ_HUMAN TCPZ_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). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:25467444</ref> [[http://www.uniprot.org/uniprot/TCPG_HUMAN TCPG_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> [[http://www.uniprot.org/uniprot/TCPH_HUMAN TCPH_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). The TRiC complex plays a role in the folding of actin and tubulin (Probable).<ref>PMID:25467444</ref> [[http://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> [[http://www.uniprot.org/uniprot/TCPQ_HUMAN TCPQ_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> [[http://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> [[http://www.uniprot.org/uniprot/TCPD_HUMAN TCPD_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> [[http://www.uniprot.org/uniprot/TCPE_HUMAN TCPE_HUMAN]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin.<ref>PMID:20080638</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6nra" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Aebersold, R]] | ||
[[Category: Chiu, W]] | [[Category: Chiu, W]] | ||
| + | [[Category: Frydman, J]] | ||
| + | [[Category: Gestaut, D R]] | ||
| + | [[Category: Joachimiak, L A]] | ||
[[Category: Leitner, A]] | [[Category: Leitner, A]] | ||
| - | [[Category: Joachimiak, L.A]] | ||
| - | [[Category: Gestaut, D.R]] | ||
| - | [[Category: Walzthoeni, T]] | ||
| - | [[Category: Pintilie, G]] | ||
[[Category: Ma, B]] | [[Category: Ma, B]] | ||
| - | [[Category: | + | [[Category: Pintilie, G]] |
| - | [[Category: | + | [[Category: Roh, S H]] |
| - | [[Category: | + | [[Category: Walzthoeni, T]] |
| + | [[Category: Chaperone]] | ||
| + | [[Category: Cryoem]] | ||
| + | [[Category: Molecular chaperone]] | ||
| + | [[Category: Pfd]] | ||
| + | [[Category: Protein folding]] | ||
| + | [[Category: Tric/cct]] | ||
Revision as of 06:05, 19 June 2019
hTRiC-hPFD Class1 (No PFD)
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Categories: Large Structures | Aebersold, R | Chiu, W | Frydman, J | Gestaut, D R | Joachimiak, L A | Leitner, A | Ma, B | Pintilie, G | Roh, S H | Walzthoeni, T | Chaperone | Cryoem | Molecular chaperone | Pfd | Protein folding | Tric/cct
