4v8r: Difference between revisions
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==The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning== | ==The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning== | ||
<StructureSection load='4v8r' size='340' side='right' caption='[[4v8r]], [[Resolution|resolution]] 3.80Å' scene=''> | <StructureSection load='4v8r' size='340' side='right'caption='[[4v8r]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v8r]] is a 32 chain structure. This structure supersedes | <table><tr><td colspan='2'>[[4v8r]] is a 32 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4aol 4aol] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4apk 4apk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V8R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V8R 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=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p9d|3p9d]], [[4b2t|4b2t]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p9d|3p9d]], [[4b2t|4b2t]]</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=4v8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v8r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v8r RCSB], [http://www.ebi.ac.uk/pdbsum/4v8r PDBsum]</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=4v8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v8r OCA], [http://pdbe.org/4v8r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v8r RCSB], [http://www.ebi.ac.uk/pdbsum/4v8r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v8r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[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/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/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/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/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/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/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/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/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/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/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/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/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/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/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. | ||
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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 4v8r" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Chaperonin 3D structures|Chaperonin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | |||
[[Category: Large Structures]] | |||
[[Category: Kalisman, N]] | [[Category: Kalisman, N]] | ||
[[Category: Levitt, M]] | [[Category: Levitt, M]] | ||
[[Category: Schroder, G F]] | [[Category: Schroder, G F]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
