5cya
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cya]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CYA FirstGlance]. <br> | <table><tr><td colspan='2'>[[5cya]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CYA FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5cya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cya OCA], [https://pdbe.org/5cya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cya RCSB], [https://www.ebi.ac.uk/pdbsum/5cya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cya ProSAT]</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=5cya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cya OCA], [https://pdbe.org/5cya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cya RCSB], [https://www.ebi.ac.uk/pdbsum/5cya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cya ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TBCC_YEAST TBCC_YEAST] Tubulin-folding protein; involved in the early step of the tubulin folding pathway. | [https://www.uniprot.org/uniprot/TBCC_YEAST TBCC_YEAST] Tubulin-folding protein; involved in the early step of the tubulin folding pathway. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Microtubule dynamics and polarity stem from the polymerization of alphass-tubulin heterodimers. Five conserved tubulin cofactors/chaperones and the Arl2 GTPase regulate alpha- and beta-tubulin assembly into heterodimers and maintain the soluble tubulin pool in the cytoplasm, but their physical mechanisms are unknown. Here, we reconstitute a core tubulin chaperone consisting of tubulin cofactors TBCD, TBCE and Arl2, and reveal a cage-like structure for regulating alphabeta-tubulin. Biochemical assays and electron microscopy structures of multiple intermediates show the sequential binding of alphabeta-tubulin dimer followed by tubulin cofactor TBCC onto this chaperone, forming a ternary complex in which Arl2 GTP hydrolysis is activated to alter alphabeta-tubulin conformation. A GTP-state locked Arl2 mutant inhibits ternary complex dissociation in vitro and causes severe defects in microtubule dynamics in vivo. Our studies suggest a revised paradigm for tubulin cofactors and Arl2 functions as a catalytic chaperone that regulates soluble alphabeta-tubulin assembly and maintenance to support microtubule dynamics. | ||
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| - | Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble alphabeta-tubulin pool for microtubule dynamics.,Nithiananatham S, Le S, Seto E, Jia W, Leary J, Corbett KD, Moore JK, Al-Bassam J Elife. 2015 Jul 24;4. doi: 10.7554/eLife.08811. PMID:26208336<ref>PMID:26208336</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5cya" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of Arl2 GTPase-activating protein tubulin cofactor C (TBCC)
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