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4v81

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{{Large structure}}
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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==
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<StructureSection load='4v81' size='340' side='right' caption='[[4v81]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
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<StructureSection load='4v81' size='340' side='right'caption='[[4v81]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4v81]] is a 32 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. This structure supersedes and combines 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V81 FirstGlance]. <br>
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<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>
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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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCT1, TCP1, YD8142.13, YD8142B.04, YDR212W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), BIN3, CCT2, TCP2, YIL142W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), BIN2, CCT3, J1336, TCP3, YJL014W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), ANC2, CCT4, TCP4, YDL143W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), CCT5, J1752, TCP5, YJR064W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), CCT6, TCP20, TCP6, YD9395.21, YDR188W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), CCT7, J0804, YJL111W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), CCT8, J1374, YJL008C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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<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>
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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=4v81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v81 OCA], [http://pdbe.org/4v81 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v81 RCSB], [http://www.ebi.ac.uk/pdbsum/4v81 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v81 ProSAT]</span></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=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>
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{{Large structure}}
 
== Function ==
== Function ==
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[[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.
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[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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</div>
</div>
<div class="pdbe-citations 4v81" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4v81" 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: Atcc 18824]]
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[[Category: Large Structures]]
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[[Category: Beuron, F]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Dekker, C]]
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[[Category: Beuron F]]
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[[Category: McCormack, E A]]
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[[Category: Dekker C]]
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[[Category: Pearl, L H]]
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[[Category: McCormack EA]]
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[[Category: Roe, S M]]
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[[Category: Pearl LH]]
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[[Category: Willison, K R]]
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[[Category: Roe SM]]
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[[Category: Actin/tubulin binding]]
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[[Category: Willison KR]]
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[[Category: Chaperone]]
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[[Category: Eukaryotic chaperonin]]
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[[Category: Hexadecamer]]
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[[Category: Hsp60]]
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Current revision

The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins

PDB ID 4v81

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