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| | <StructureSection load='5cya' size='340' side='right'caption='[[5cya]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5cya' size='340' side='right'caption='[[5cya]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cya]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. 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> | + | <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"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CIN2, YPL241C, P1043 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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'>[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://pdbe.org/5cya PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cya RCSB], [http://www.ebi.ac.uk/pdbsum/5cya PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cya ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Al-Bassam, J]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Corbett, K D]] | + | [[Category: Al-Bassam J]] |
| - | [[Category: Jia, W]] | + | [[Category: Corbett KD]] |
| - | [[Category: Le, S]] | + | [[Category: Jia W]] |
| - | [[Category: Leary, J]] | + | [[Category: Le S]] |
| - | [[Category: Moore, J K]] | + | [[Category: Leary J]] |
| - | [[Category: Nithianantham, S]] | + | [[Category: Moore JK]] |
| - | [[Category: Seto, E]] | + | [[Category: Nithianantham S]] |
| - | [[Category: Arl2 gtpase-activating protein tbcc]]
| + | [[Category: Seto E]] |
| - | [[Category: Beta helix]]
| + | |
| - | [[Category: Beta-sheet]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Gap activity]]
| + | |
| - | [[Category: Mirotubule dynamic]]
| + | |
| - | [[Category: Tubulin chaperone]]
| + | |
| - | [[Category: Tubulin cofactor]]
| + | |
| Structural highlights
Function
TBCC_YEAST Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nithiananatham S, Le S, Seto E, Jia W, Leary J, Corbett KD, Moore JK, Al-Bassam J. Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble alphabeta-tubulin pool for microtubule dynamics. Elife. 2015 Jul 24;4. doi: 10.7554/eLife.08811. PMID:26208336 doi:http://dx.doi.org/10.7554/eLife.08811
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