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6ys4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Homo sapiens SAS-6 coiled-coil domain== | |
| + | <StructureSection load='6ys4' size='340' side='right'caption='[[6ys4]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ys4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YS4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SASS6, SAS6 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6ys4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ys4 OCA], [https://pdbe.org/6ys4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ys4 RCSB], [https://www.ebi.ac.uk/pdbsum/6ys4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ys4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[https://www.uniprot.org/uniprot/SAS6_HUMAN SAS6_HUMAN]] Autosomal recessive primary microcephaly. The disease is caused by variants affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/SAS6_HUMAN SAS6_HUMAN]] Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication: required both for mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. Overexpression results in excess foci-bearing centriolar markers. Required for the recruitment of STIL to the procentriole and for STIL-mediated centriole amplification (PubMed:22020124).<ref>PMID:15665853</ref> <ref>PMID:16244668</ref> <ref>PMID:17681131</ref> <ref>PMID:22020124</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Centrioles are eukaryotic organelles that template the formation of cilia and flagella, as well as organize the microtubule network and the mitotic spindle in animal cells. Centrioles have proximal-distal polarity and a 9-fold radial symmetry imparted by a likewise symmetrical central scaffold, the cartwheel. The spindle assembly abnormal protein 6 (SAS-6) self-assembles into 9-fold radially symmetric ring-shaped oligomers that stack via an unknown mechanism to form the cartwheel. Here, we uncover a homo-oligomerization interaction mediated by the coiled-coil domain of SAS-6. Crystallographic structures of Chlamydomonas reinhardtii SAS-6 coiled-coil complexes suggest this interaction is asymmetric, thereby imparting polarity to the cartwheel. Using a cryoelectron microscopy (cryo-EM) reconstitution assay, we demonstrate that amino acid substitutions disrupting this asymmetric association also impair SAS-6 ring stacking. Our work raises the possibility that the asymmetric interaction inherent to SAS-6 coiled-coil provides a polar element for cartwheel assembly, which may assist the establishment of the centriolar proximal-distal axis. | ||
| - | + | Structures of SAS-6 coiled coil hold implications for the polarity of the centriolar cartwheel.,Kantsadi AL, Hatzopoulos GN, Gonczy P, Vakonakis I Structure. 2022 Feb 22. pii: S0969-2126(22)00041-7. doi:, 10.1016/j.str.2022.02.005. PMID:35240058<ref>PMID:35240058</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6ys4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kantsadi, A L]] | ||
[[Category: Vakonakis, I]] | [[Category: Vakonakis, I]] | ||
| - | [[Category: | + | [[Category: Alpha helical]] |
| + | [[Category: Cartwheel]] | ||
| + | [[Category: Centriole]] | ||
| + | [[Category: Centrosome]] | ||
| + | [[Category: Coiled coil]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Structural protein]] | ||
Current revision
Structure of the Homo sapiens SAS-6 coiled-coil domain
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