4ynh

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m (Protected "4ynh" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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==Structure of the C. elegans SAS-5 Implico dimerization domain==
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<StructureSection load='4ynh' size='340' side='right' caption='[[4ynh]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ynh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YNH FirstGlance]. <br>
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</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=4ynh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ynh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ynh RCSB], [http://www.ebi.ac.uk/pdbsum/4ynh PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4ynh is ON HOLD until Paper Publication
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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>
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Authors: Rogala, K.B., Vakonakis, I., Hatzopoulos, G.N.
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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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Description: Structure of a C. elegans protein
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Hatzopoulos, G N]]
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[[Category: Rogala, K B]]
[[Category: Vakonakis, I]]
[[Category: Vakonakis, I]]
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[[Category: Hatzopoulos, G.N]]
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[[Category: Centriole]]
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[[Category: Rogala, K.B]]
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[[Category: Dimerization domain]]
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[[Category: Sas-5]]
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[[Category: Structural protein]]

Revision as of 13:58, 10 June 2015

Structure of the C. elegans SAS-5 Implico dimerization domain

4ynh, resolution 1.00Å

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