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| ==N-terminal fragment of Drosophila melanogaster Sas-6 (F143D), dimerised via the coiled-coil domain.== | | ==N-terminal fragment of Drosophila melanogaster Sas-6 (F143D), dimerised via the coiled-coil domain.== |
- | <StructureSection load='5al7' size='340' side='right' caption='[[5al7]], [[Resolution|resolution]] 2.92Å' scene=''> | + | <StructureSection load='5al7' size='340' side='right'caption='[[5al7]], [[Resolution|resolution]] 2.92Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5al7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AL7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AL7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5al7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AL7 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5al6|5al6]]</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=5al7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5al7 OCA], [https://pdbe.org/5al7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5al7 RCSB], [https://www.ebi.ac.uk/pdbsum/5al7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5al7 ProSAT]</span></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=5al7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5al7 OCA], [http://pdbe.org/5al7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5al7 RCSB], [http://www.ebi.ac.uk/pdbsum/5al7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5al7 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/SAS6_DROME SAS6_DROME]] Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication.<ref>PMID:17412918</ref> <ref>PMID:17463247</ref> | + | [https://www.uniprot.org/uniprot/SAS6_DROME SAS6_DROME] Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication.<ref>PMID:17412918</ref> <ref>PMID:17463247</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
- | [[Category: Cottee, M A]] | + | [[Category: Large Structures]] |
- | [[Category: Johnson, S]] | + | [[Category: Cottee MA]] |
- | [[Category: Lea, S M]] | + | [[Category: Johnson S]] |
- | [[Category: Cartwheel]] | + | [[Category: Lea SM]] |
- | [[Category: Centriole]]
| + | |
- | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
SAS6_DROME Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication.[1] [2]
Publication Abstract from PubMed
Sas-6 and Ana2/STIL proteins are required for centriole duplication and the homo-oligomerisation properties of Sas-6 help establish the nine-fold symmetry of the central cartwheel that initiates centriole assembly. Ana2/STIL proteins are poorly conserved, but they all contain a predicted Central Coiled-Coil Domain (CCCD). Here we show that the Drosophila Ana2 CCCD forms a tetramer, and we solve its structure to 0.8 A, revealing that it adopts an unusual parallel-coil topology. We also solve the structure of the Drosophila Sas-6 N-terminal domain to 2.9 A revealing that it forms higher-order oligomers through canonical interactions. Point mutations that perturb Sas-6 or Ana2 homo-oligomerisation in vitro strongly perturb centriole assembly in vivo. Thus, efficient centriole duplication in flies requires the homo-oligomerisation of both Sas-6 and Ana2, and the Ana2 CCCD tetramer structure provides important information on how these proteins might cooperate to form a cartwheel structure.
The homo-oligomerisation of both Sas-6 and Ana2 is required for efficient centriole assembly in flies.,Cottee MA, Muschalik N, Johnson S, Leveson J, Raff JW, Lea SM Elife. 2015 May 23;4. doi: 10.7554/eLife.07236. PMID:26002084[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goshima G, Wollman R, Goodwin SS, Zhang N, Scholey JM, Vale RD, Stuurman N. Genes required for mitotic spindle assembly in Drosophila S2 cells. Science. 2007 Apr 20;316(5823):417-21. Epub 2007 Apr 5. PMID:17412918 doi:http://dx.doi.org/1141314
- ↑ Rodrigues-Martins A, Riparbelli M, Callaini G, Glover DM, Bettencourt-Dias M. Revisiting the role of the mother centriole in centriole biogenesis. Science. 2007 May 18;316(5827):1046-50. Epub 2007 Apr 26. PMID:17463247 doi:http://dx.doi.org/10.1126/science.1142950
- ↑ Cottee MA, Muschalik N, Johnson S, Leveson J, Raff JW, Lea SM. The homo-oligomerisation of both Sas-6 and Ana2 is required for efficient centriole assembly in flies. Elife. 2015 May 23;4. doi: 10.7554/eLife.07236. PMID:26002084 doi:http://dx.doi.org/10.7554/eLife.07236
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