5cya: Difference between revisions
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''' | ==Crystal structure of Arl2 GTPase-activating protein tubulin cofactor C (TBCC)== | ||
<StructureSection load='5cya' size='340' side='right' caption='[[5cya]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5cya]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CYA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=5cya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cya OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5cya RCSB], [http://www.ebi.ac.uk/pdbsum/5cya PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Al-Bassam, J]] | [[Category: Al-Bassam, J]] | ||
[[Category: | [[Category: Corbett, K D]] | ||
[[Category: Jia, W]] | [[Category: Jia, W]] | ||
[[Category: Le, S]] | [[Category: Le, S]] | ||
[[Category: Leary, J]] | |||
[[Category: Moore, J K]] | |||
[[Category: Nithianantham, S]] | [[Category: Nithianantham, S]] | ||
[[Category: Seto, E]] | [[Category: Seto, E]] | ||
[[Category: Arl2 gtpase-activating protein tbcc]] | |||
[[Category: Beta helix]] | |||
[[Category: Beta-sheet]] | |||
[[Category: Chaperone]] | |||
[[Category: Gap activity]] | |||
[[Category: Mirotubule dynamic]] | |||
[[Category: Tubulin chaperone]] | |||
[[Category: Tubulin cofactor]] | |||
