5cya

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==Crystal structure of Arl2 GTPase-activating protein tubulin cofactor C (TBCC)==
==Crystal structure of Arl2 GTPase-activating protein tubulin cofactor C (TBCC)==
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<StructureSection load='5cya' size='340' side='right' caption='[[5cya]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='5cya' size='340' side='right'caption='[[5cya]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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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]] 2&#8491;</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=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>
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<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>
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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=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 ==
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[[http://www.uniprot.org/uniprot/TBCC_YEAST TBCC_YEAST]] Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
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[https://www.uniprot.org/uniprot/TBCC_YEAST TBCC_YEAST] Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Al-Bassam, J]]
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[[Category: Large Structures]]
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[[Category: Corbett, K D]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Jia, W]]
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[[Category: Al-Bassam J]]
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[[Category: Le, S]]
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[[Category: Corbett KD]]
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[[Category: Leary, J]]
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[[Category: Jia W]]
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[[Category: Moore, J K]]
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[[Category: Le S]]
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[[Category: Nithianantham, S]]
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[[Category: Leary J]]
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[[Category: Seto, E]]
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[[Category: Moore JK]]
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[[Category: Arl2 gtpase-activating protein tbcc]]
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[[Category: Nithianantham S]]
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[[Category: Beta helix]]
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[[Category: Seto E]]
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[[Category: Beta-sheet]]
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[[Category: Chaperone]]
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[[Category: Gap activity]]
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[[Category: Mirotubule dynamic]]
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[[Category: Tubulin chaperone]]
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[[Category: Tubulin cofactor]]
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Current revision

Crystal structure of Arl2 GTPase-activating protein tubulin cofactor C (TBCC)

PDB ID 5cya

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