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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== |
| - | <StructureSection load='3pyi' size='340' side='right' caption='[[3pyi]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3pyi' size='340' side='right'caption='[[3pyi]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pyi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. 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> | + | <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> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.104Å</td></tr> |
| - | <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 CAEEL])</td></tr> | + | <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> |
| - | <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://pdbe.org/3pyi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pyi RCSB], [http://www.ebi.ac.uk/pdbsum/3pyi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pyi ProSAT]</span></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=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> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SAS6_CAEEL SAS6_CAEEL]] Required for centrosome duplication. Participates in centriole assembly.<ref>PMID:15572125</ref> <ref>PMID:15665853</ref> | + | [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> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3pyi" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| - | [[Category: Steinmetz, M O]] | + | [[Category: Large Structures]] |
| - | [[Category: Vakonakis, I]] | + | [[Category: Steinmetz MO]] |
| - | [[Category: Alpha-beta protein]] | + | [[Category: Vakonakis I]] |
| - | [[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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