4v94

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{{Large structure}}
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==Molecular architecture of the eukaryotic chaperonin TRiC/CCT derived by a combination of chemical crosslinking and mass-spectrometry, XL-MS==
==Molecular architecture of the eukaryotic chaperonin TRiC/CCT derived by a combination of chemical crosslinking and mass-spectrometry, XL-MS==
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<StructureSection load='4v94' size='340' side='right' caption='[[4v94]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
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<StructureSection load='4v94' size='340' side='right'caption='[[4v94]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4v94]] is a 32 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d8q 4d8q] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d8r 4d8r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V94 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4v94]] is a 32 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d8q 4d8q] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d8r 4d8r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V94 FirstGlance]. <br>
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</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p9d|3p9d]], [[3p9e|3p9e]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4v94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v94 OCA], [https://pdbe.org/4v94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v94 RCSB], [https://www.ebi.ac.uk/pdbsum/4v94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v94 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCT6, TCP20, TCP6, YD9395.21, YDR188W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), CCT8, J1374, YJL008C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), CCT7, J0804, YJL111W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), CCT5, J1752, TCP5, YJR064W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), BIN3, CCT2, TCP2, YIL142W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), ANC2, CCT4, TCP4, YDL143W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), CCT1, TCP1, YD8142.13, YD8142B.04, YDR212W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), BIN2, CCT3, J1336, TCP3, YJL014W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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<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=4v94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v94 OCA], [http://pdbe.org/4v94 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v94 RCSB], [http://www.ebi.ac.uk/pdbsum/4v94 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v94 ProSAT]</span></td></tr>
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</table>
</table>
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{{Large structure}}
 
== Function ==
== Function ==
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[[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/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/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/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/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/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/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. [[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.
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[https://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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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.
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TRiC/CCT is a highly conserved and essential chaperonin that uses ATP cycling to facilitate folding of approximately 10% of the eukaryotic proteome. This 1 MDa hetero-oligomeric complex consists of two stacked rings of eight paralogous subunits each. Previously proposed TRiC models differ substantially in their subunit arrangements and ring register. Here, we integrate chemical crosslinking, mass spectrometry, and combinatorial modeling to reveal the definitive subunit arrangement of TRiC. In vivo disulfide mapping provided additional validation for the crosslinking-derived arrangement as the definitive TRiC topology. This subunit arrangement allowed the refinement of a structural model using existing X-ray diffraction data. The structure described here explains all available crosslink experiments, provides a rationale for previously unexplained structural features, and reveals a surprising asymmetry of charges within the chaperonin folding chamber.
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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<ref>PMID:21701561</ref>
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The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.,Leitner A, Joachimiak LA, Bracher A, Monkemeyer L, Walzthoeni T, Chen B, Pechmann S, Holmes S, Cong Y, Ma B, Ludtke S, Chiu W, Hartl FU, Aebersold R, Frydman J Structure. 2012 May 9;20(5):814-25. Epub 2012 Apr 12. PMID:22503819<ref>PMID:22503819</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4v94" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4v94" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
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[[Category: Large Structures]]
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[[Category: Aebersold, R]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Bracher, A]]
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[[Category: Aebersold R]]
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[[Category: Chen, B]]
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[[Category: Bracher A]]
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[[Category: Chiu, W]]
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[[Category: Chen B]]
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[[Category: Cong, Y]]
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[[Category: Chiu W]]
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[[Category: Frydman, J]]
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[[Category: Cong Y]]
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[[Category: Hartl, F U]]
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[[Category: Frydman J]]
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[[Category: Holmes, S]]
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[[Category: Hartl FU]]
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[[Category: Joachimiak, L A]]
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[[Category: Holmes S]]
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[[Category: Leitner, A]]
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[[Category: Joachimiak LA]]
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[[Category: Ludtke, S]]
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[[Category: Leitner A]]
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[[Category: Ma, B]]
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[[Category: Ludtke S]]
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[[Category: Monkemeyer, L]]
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[[Category: Ma B]]
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[[Category: Pechmann, S]]
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[[Category: Monkemeyer L]]
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[[Category: Walzthoeni, T]]
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[[Category: Pechmann S]]
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[[Category: Atpase]]
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[[Category: Walzthoeni T]]
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[[Category: Chaperone]]
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[[Category: Chaperonin]]
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[[Category: Cytosol]]
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[[Category: Molecular chaperone]]
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[[Category: Nano cage]]
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[[Category: Protein folding]]
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Revision as of 08:13, 29 March 2023

Molecular architecture of the eukaryotic chaperonin TRiC/CCT derived by a combination of chemical crosslinking and mass-spectrometry, XL-MS

PDB ID 4v94

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