View source for 4yv4


==Structure of the C. elegans SAS-5 coiled coil domain==
<StructureSection load='4yv4' size='340' side='right'caption='[[4yv4]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yv4]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4YV4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <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=4yv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yv4 OCA], [https://pdbe.org/4yv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yv4 RCSB], [https://www.ebi.ac.uk/pdbsum/4yv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yv4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://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 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yv4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Hatzopoulos GN]]
[[Category: Rogala KB]]
[[Category: Vakonakis I]]