3pyi

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==Structure of the N-terminal domain of C. elegans SAS-6==
==Structure of the N-terminal domain of C. elegans SAS-6==
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<StructureSection load='3pyi' size='340' side='right' caption='[[3pyi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='3pyi' size='340' side='right'caption='[[3pyi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pyi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PYI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PYI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pyi]] is a 2 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=3PYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PYI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.104&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sas-6, Y45F10D.9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
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<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=3pyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pyi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pyi RCSB], [http://www.ebi.ac.uk/pdbsum/3pyi PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pyi OCA], [https://pdbe.org/3pyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pyi RCSB], [https://www.ebi.ac.uk/pdbsum/3pyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pyi ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/SAS6_CAEEL SAS6_CAEEL] Required for centrosome duplication. Participates in centriole assembly.<ref>PMID:15572125</ref> <ref>PMID:15665853</ref>
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The centriole, and the related basal body, is an ancient organelle characterized by a universal 9-fold radial symmetry and is critical for generating cilia, flagella, and centrosomes. The mechanisms directing centriole formation are incompletely understood and represent a fundamental open question in biology. Here, we demonstrate that the centriolar protein SAS-6 forms rod-shaped homodimers that interact through their N-terminal domains to form oligomers. We establish that such oligomerization is essential for centriole formation in C. elegans and human cells. We further generate a structural model of the related protein Bld12p from C. reinhardtii, in which nine homodimers assemble into a ring from which nine coiled-coil rods radiate outward. Moreover, we demonstrate that recombinant Bld12p self-assembles into structures akin to the central hub of the cartwheel, which serves as a scaffold for centriole formation. Overall, our findings establish a structural basis for the universal 9-fold symmetry of centrioles.
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Structural basis of the 9-fold symmetry of centrioles.,Kitagawa D, Vakonakis I, Olieric N, Hilbert M, Keller D, Olieric V, Bortfeld M, Erat MC, Fluckiger I, Gonczy P, Steinmetz MO Cell. 2011 Feb 4;144(3):364-75. PMID:21277013<ref>PMID:21277013</ref>
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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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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
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[[Category: Steinmetz, M O]]
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[[Category: Large Structures]]
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[[Category: Vakonakis, I]]
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[[Category: Steinmetz MO]]
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[[Category: Alpha-beta protein]]
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[[Category: Vakonakis I]]
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[[Category: Beta-sandwich]]
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[[Category: Centriolar]]
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[[Category: Cytoplasmic]]
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[[Category: Dimer]]
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[[Category: Structural protein]]
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Structure of the N-terminal domain of C. elegans SAS-6

PDB ID 3pyi

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