4yv4
From Proteopedia
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| - | ''' | + | ==Structure of the C. elegans SAS-5 coiled coil domain== |
| + | <StructureSection load='4yv4' size='340' side='right' caption='[[4yv4]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4yv4]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YV4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YV4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ynh|4ynh]]</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=4yv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yv4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yv4 RCSB], [http://www.ebi.ac.uk/pdbsum/4yv4 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SAS5_CAEEL SAS5_CAEEL]] Required for centrosome duplication. Essential for daughter-centriole formation. Requires both maternal and partenal expression, suggesting that it regulates centriole duplication during both spermatogenesis and early embryogenesis.<ref>PMID:15232593</ref> <ref>PMID:15572125</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Centrioles are microtubule-based organelles crucial for cell division, sensing and motility. In C. elegans, the onset of centriole formation requires notably the proteins SAS-5 and SAS-6, which have functional homologs across eukaryotic evolution. Whereas the molecular architecture of SAS-6 and its role in initiating centriole formation are well understood, the mechanisms by which SAS-5 and its relatives function is unclear. Here, we combine biophysical and structural analysis to uncover the architecture of SAS-5 and examine its functional implications in vivo. Our work reveals that two distinct self-associating domains are necessary to form higher-order oligomers of SAS-5: a trimeric coiled coil and a novel globular dimeric Implico domain. Disruption of either domain leads to centriole duplication failure in worm embryos, indicating that large SAS-5 assemblies are necessary for function in vivo. | ||
| - | The | + | The protein SAS-5 forms large oligomeric assemblies critical for centriole formation.,Rogala KB, Dynes NJ, Hatzopoulos GN, Yan J, Pong SK, Robinson CV, Deane CM, Gonczy P, Vakonakis I Elife. 2015 May 29;4. doi: 10.7554/eLife.07410. PMID:26023830<ref>PMID:26023830</ref> |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hatzopoulos, G N]] | ||
| + | [[Category: Rogala, K B]] | ||
[[Category: Vakonakis, I]] | [[Category: Vakonakis, I]] | ||
| - | [[Category: | + | [[Category: A-helical]] |
| - | [[Category: | + | [[Category: Cell cycle]] |
| + | [[Category: Coiled coil]] | ||
| + | [[Category: Structural protein]] | ||
| + | [[Category: Trimer]] | ||
Revision as of 14:00, 10 June 2015
Structure of the C. elegans SAS-5 coiled coil domain
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