4yv4: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | ==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
| ||||||||||||
