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| - | ==N-TERMINAL HEAD DOMAIN AND BEGINNING OF COILED COIL DOMAIN OF DANIO RERIO SAS-6== | + | |
| - | <StructureSection load='2y3w' size='340' side='right' caption='[[2y3w]], [[Resolution|resolution]] 1.98Å' scene=''> | + | ==N-terminal head domain and beginning of coiled coil domain of Danio rerio SAS-6== |
| | + | <StructureSection load='2y3w' size='340' side='right'caption='[[2y3w]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2y3w]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y3W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y3w]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y3W FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2y3v|2y3v]]</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]] 1.98Å</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=2y3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y3w RCSB], [http://www.ebi.ac.uk/pdbsum/2y3w PDBsum]</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=2y3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y3w OCA], [https://pdbe.org/2y3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y3w RCSB], [https://www.ebi.ac.uk/pdbsum/2y3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y3w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SAS6_DANRE SAS6_DANRE]] 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.<ref>PMID:21273447</ref> | + | [https://www.uniprot.org/uniprot/SAS6_DANRE SAS6_DANRE] 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.<ref>PMID:21273447</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2y3w" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Danio rerio]] | | [[Category: Danio rerio]] |
| - | [[Category: Breugel, M Van]] | + | [[Category: Large Structures]] |
| - | [[Category: Basal body]] | + | [[Category: Van Breugel M]] |
| - | [[Category: Cartwheel]]
| + | |
| - | [[Category: Cartwheel hub]]
| + | |
| - | [[Category: Centriole]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
SAS6_DANRE 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.[1]
Publication Abstract from PubMed
Centrioles are cylindrical, nine-fold symmetrical structures with peripheral triplet microtubules strictly required to template cilia and flagella. The highly conserved protein SAS-6 constitutes the center of the cartwheel assembly that scaffolds centrioles early in their biogenesis. We determined the x-ray structure of the N-terminal domain of SAS-6 from zebrafish and show that recombinant SAS-6 self-associates in vitro into assemblies that resemble cartwheel centers. Point mutations are consistent with the notion that centriole formation in vivo depends on the interactions that define the self-assemblies observed here. Thus, these interactions are likely essential to the structural organization of cartwheel centers.
Structures of SAS-6 Suggest Its Organization in Centrioles.,van Breugel M, Hirono M, Andreeva A, Yanagisawa HA, Yamaguchi S, Nakazawa Y, Morgner N, Petrovich M, Ebong IO, Robinson CV, Johnson CM, Veprintsev D, Zuber B Science. 2011 Jan 27. PMID:21273447[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Breugel M, Hirono M, Andreeva A, Yanagisawa HA, Yamaguchi S, Nakazawa Y, Morgner N, Petrovich M, Ebong IO, Robinson CV, Johnson CM, Veprintsev D, Zuber B. Structures of SAS-6 Suggest Its Organization in Centrioles. Science. 2011 Jan 27. PMID:21273447 doi:10.1126/science.1199325
- ↑ van Breugel M, Hirono M, Andreeva A, Yanagisawa HA, Yamaguchi S, Nakazawa Y, Morgner N, Petrovich M, Ebong IO, Robinson CV, Johnson CM, Veprintsev D, Zuber B. Structures of SAS-6 Suggest Its Organization in Centrioles. Science. 2011 Jan 27. PMID:21273447 doi:10.1126/science.1199325
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