|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of Human T-complex protein 1 subunit epsilon (CCT5) mutant His147Arg== | | ==Structure of Human T-complex protein 1 subunit epsilon (CCT5) mutant His147Arg== |
| - | <StructureSection load='5uyz' size='340' side='right' caption='[[5uyz]], [[Resolution|resolution]] 3.60Å' scene=''> | + | <StructureSection load='5uyz' size='340' side='right'caption='[[5uyz]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5uyz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UYZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UYZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uyz]] is a 4 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=5UYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UYZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uyx|5uyx]]</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCT5, CCTE, KIAA0098 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5uyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uyz OCA], [https://pdbe.org/5uyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uyz RCSB], [https://www.ebi.ac.uk/pdbsum/5uyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uyz ProSAT]</span></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=5uyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uyz OCA], [http://pdbe.org/5uyz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uyz RCSB], [http://www.ebi.ac.uk/pdbsum/5uyz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uyz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == 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. | + | [https://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 == | | == Function == |
| - | [[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> | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Adams, P D]] | + | [[Category: Large Structures]] |
| - | [[Category: King, J A]] | + | [[Category: Adams PD]] |
| - | [[Category: McAndrew, R P]] | + | [[Category: King JA]] |
| - | [[Category: Pereira, J H]] | + | [[Category: McAndrew RP]] |
| - | [[Category: Ralston, C Y]] | + | [[Category: Pereira JH]] |
| - | [[Category: Sergeeva, O A]] | + | [[Category: Ralston CY]] |
| - | [[Category: Chaperonin hexadecameric complex atp-dependent cct5 gene]] | + | [[Category: Sergeeva OA]] |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Disease
TCPE_HUMAN Hereditary sensory and autonomic neuropathy with spastic paraplegia. The disease is caused by mutations affecting the gene represented in this entry.
Function
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.[1]
Publication Abstract from PubMed
The human chaperonin TRiC consists of eight non-identical subunits, and its protein-folding activity is critical for cellular health. Misfolded proteins are associated with many human diseases, such as amyloid diseases, cancer, and neuropathies, making TRiC a potential therapeutic target. A detailed structural understanding of its ATP-dependent folding mechanism and substrate recognition is therefore of great importance. Of particular health-related interest is the mutation Histidine 147 to Arginine (H147R) in human TRiC subunit 5 (CCT5), which has been associated with hereditary sensory neuropathy. In this paper, we describe the crystal structures of CCT5 and the CCT5-H147R mutant, which provide important structural information for this vital protein-folding machine in humans. This first X-ray crystallographic study of a single human CCT subunit in the context of a hexadecameric complex can be expanded in the future to the other 7 subunits that form the TRiC complex.
Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.,Pereira JH, McAndrew RP, Sergeeva OA, Ralston CY, King JA, Adams PD Sci Rep. 2017 Jun 16;7(1):3673. doi: 10.1038/s41598-017-03825-3. PMID:28623285[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Seo S, Baye LM, Schulz NP, Beck JS, Zhang Q, Slusarski DC, Sheffield VC. BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly. Proc Natl Acad Sci U S A. 2010 Jan 4. PMID:20080638 doi:http://dx.doi.org/0910268107
- ↑ Pereira JH, McAndrew RP, Sergeeva OA, Ralston CY, King JA, Adams PD. Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy. Sci Rep. 2017 Jun 16;7(1):3673. doi: 10.1038/s41598-017-03825-3. PMID:28623285 doi:http://dx.doi.org/10.1038/s41598-017-03825-3
|
