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| | ==The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins== | | ==The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins== |
| - | <StructureSection load='4v81' size='340' side='right' caption='[[4v81]], [[Resolution|resolution]] 3.80Å' scene=''> | + | <StructureSection load='4v81' size='340' side='right'caption='[[4v81]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v81]] is a 32 chain structure. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3p9e 3p9e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V81 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V81 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v81]] is a 32 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3p9d 3p9d] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3p9e 3p9e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V81 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=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p9d|3p9d]], [[3p9e|3p9e]]</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=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4v81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v81 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v81 RCSB], [http://www.ebi.ac.uk/pdbsum/4v81 PDBsum]</span></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=4v81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v81 OCA], [https://pdbe.org/4v81 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v81 RCSB], [https://www.ebi.ac.uk/pdbsum/4v81 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v81 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TCPZ_YEAST TCPZ_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPG_YEAST TCPG_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPH_YEAST TCPH_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity). [[http://www.uniprot.org/uniprot/TCPB_YEAST TCPB_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPQ_YEAST TCPQ_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity). [[http://www.uniprot.org/uniprot/TCPA_YEAST TCPA_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPD_YEAST TCPD_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [[http://www.uniprot.org/uniprot/TCPE_YEAST TCPE_YEAST]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. | + | [https://www.uniprot.org/uniprot/TCPA_YEAST TCPA_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4v81" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Chaperonin 3D structures|Chaperonin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beuron, F]] | + | [[Category: Large Structures]] |
| - | [[Category: Dekker, C]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: McCormack, E A]] | + | [[Category: Beuron F]] |
| - | [[Category: Pearl, L H]] | + | [[Category: Dekker C]] |
| - | [[Category: Roe, S M]] | + | [[Category: McCormack EA]] |
| - | [[Category: Willison, K R]] | + | [[Category: Pearl LH]] |
| - | [[Category: Actin/tubulin binding]] | + | [[Category: Roe SM]] |
| - | [[Category: Chaperone]] | + | [[Category: Willison KR]] |
| - | [[Category: Eukaryotic chaperonin]]
| + | |
| - | [[Category: Hexadecamer]]
| + | |
| - | [[Category: Hsp60]]
| + | |
| Structural highlights
Function
TCPA_YEAST Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
Publication Abstract from PubMed
The cytosolic chaperonin CCT is a 1-MDa protein-folding machine essential for eukaryotic life. The CCT interactome shows involvement in folding and assembly of a small range of proteins linked to essential cellular processes such as cytoskeleton assembly and cell-cycle regulation. CCT has a classic chaperonin architecture, with two heterogeneous 8-membered rings stacked back-to-back, enclosing a folding cavity. However, the mechanism by which CCT assists folding is distinct from other chaperonins, with no hydrophobic wall lining a potential Anfinsen cage, and a sequential rather than concerted ATP hydrolysis mechanism. We have solved the crystal structure of yeast CCT in complex with actin at 3.8 A resolution, revealing the subunit organisation and the location of discrete patches of co-evolving 'signature residues' that mediate specific interactions between CCT and its substrates. The intrinsic asymmetry is revealed by the structural individuality of the CCT subunits, which display unique configurations, substrate binding properties, ATP-binding heterogeneity and subunit-subunit interactions. The location of the evolutionarily conserved N-terminus of Cct5 on the outside of the barrel, confirmed by mutational studies, is unique to eukaryotic cytosolic chaperonins.
The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.,Dekker C, Roe SM, McCormack EA, Beuron F, Pearl LH, Willison KR EMBO J. 2011 Jun 24. doi: 10.1038/emboj.2011.208. PMID:21701561[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dekker C, Roe SM, McCormack EA, Beuron F, Pearl LH, Willison KR. The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins. EMBO J. 2011 Jun 24. doi: 10.1038/emboj.2011.208. PMID:21701561 doi:10.1038/emboj.2011.208
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