5al7: Difference between revisions
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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=''> | ||
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</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"><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='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'>[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://www.rcsb.org/pdb/explore.do?structureId=5al7 RCSB], [http://www.ebi.ac.uk/pdbsum/5al7 PDBsum]</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 == | ||
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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 5al7" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:03, 11 March 2017
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.
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 PubMedSas-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
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