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| | ==crystal structure of Sfi1p/Cdc31p complex== | | ==crystal structure of Sfi1p/Cdc31p complex== |
| - | <StructureSection load='2doq' size='340' side='right' caption='[[2doq]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='2doq' size='340' side='right'caption='[[2doq]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2doq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DOQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2doq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DOQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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='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">CDC31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), SFI1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC31 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), SFI1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2doq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2doq OCA], [http://pdbe.org/2doq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2doq RCSB], [http://www.ebi.ac.uk/pdbsum/2doq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2doq 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=2doq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2doq OCA], [https://pdbe.org/2doq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2doq RCSB], [https://www.ebi.ac.uk/pdbsum/2doq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2doq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CDC31_YEAST CDC31_YEAST]] Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB) half-bridge. At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication. It probably plays a similar role in de novo assembly of NPCs at the nuclear envelope. Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity.<ref>PMID:8188750</ref> <ref>PMID:8070654</ref> <ref>PMID:9813095</ref> <ref>PMID:11156974</ref> <ref>PMID:12486115</ref> <ref>PMID:14504268</ref> [[http://www.uniprot.org/uniprot/SFI1_YEAST SFI1_YEAST]] Component of the spindle pole body (SPB) half-bridge involved in the initial steps of SPB duplication.<ref>PMID:10455233</ref> <ref>PMID:14504268</ref> <ref>PMID:16785321</ref> | + | [[https://www.uniprot.org/uniprot/CDC31_YEAST CDC31_YEAST]] Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB) half-bridge. At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication. It probably plays a similar role in de novo assembly of NPCs at the nuclear envelope. Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity.<ref>PMID:8188750</ref> <ref>PMID:8070654</ref> <ref>PMID:9813095</ref> <ref>PMID:11156974</ref> <ref>PMID:12486115</ref> <ref>PMID:14504268</ref> [[https://www.uniprot.org/uniprot/SFI1_YEAST SFI1_YEAST]] Component of the spindle pole body (SPB) half-bridge involved in the initial steps of SPB duplication.<ref>PMID:10455233</ref> <ref>PMID:14504268</ref> <ref>PMID:16785321</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/2doq_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/2doq_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2doq" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2doq" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Nucleoporin 3D structures|Nucleoporin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 18824]] | | [[Category: Atcc 18824]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Conduit, P T]] | | [[Category: Conduit, P T]] |
| | [[Category: Kilmartin, J V]] | | [[Category: Kilmartin, J V]] |
| Structural highlights
Function
[CDC31_YEAST] Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB) half-bridge. At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication. It probably plays a similar role in de novo assembly of NPCs at the nuclear envelope. Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity.[1] [2] [3] [4] [5] [6] [SFI1_YEAST] Component of the spindle pole body (SPB) half-bridge involved in the initial steps of SPB duplication.[7] [8] [9]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Centrins are calmodulin-like proteins present in centrosomes and yeast spindle pole bodies (SPBs) and have essential functions in their duplication. The Saccharomyces cerevisiae centrin, Cdc31p, binds Sfi1p on multiple conserved repeats; both proteins localize to the SPB half-bridge, where the new SPB is assembled. The crystal structures of Sfi1p-centrin complexes containing several repeats show Sfi1p as an alpha helix with centrins wrapped around each repeat and similar centrin-centrin contacts between each repeat. Electron microscopy (EM) shadowing of an Sfi1p-centrin complex with 15 Sfi1 repeats and 15 centrins bound showed filaments 60 nm long, compatible with all the Sfi1 repeats as a continuous alpha helix. Immuno-EM localization of the Sfi1p N and C termini showed Sfi1p-centrin filaments spanning the length of the half-bridge with the Sfi1p N terminus at the SPB. This suggests a model for SPB duplication where the half-bridge doubles in length by association of the Sfi1p C termini, thereby providing a new Sfi1p N terminus to initiate SPB assembly.
Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication.,Li S, Sandercock AM, Conduit P, Robinson CV, Williams RL, Kilmartin JV J Cell Biol. 2006 Jun 19;173(6):867-77. PMID:16785321[10]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Biggins S, Rose MD. Direct interaction between yeast spindle pole body components: Kar1p is required for Cdc31p localization to the spindle pole body. J Cell Biol. 1994 May;125(4):843-52. PMID:8188750
- ↑ Vallen EA, Ho W, Winey M, Rose MD. Genetic interactions between CDC31 and KAR1, two genes required for duplication of the microtubule organizing center in Saccharomyces cerevisiae. Genetics. 1994 Jun;137(2):407-22. PMID:8070654
- ↑ Sullivan DS, Biggins S, Rose MD. The yeast centrin, cdc31p, and the interacting protein kinase, Kic1p, are required for cell integrity. J Cell Biol. 1998 Nov 2;143(3):751-65. PMID:9813095
- ↑ Ivanovska I, Rose MD. Fine structure analysis of the yeast centrin, Cdc31p, identifies residues specific for cell morphology and spindle pole body duplication. Genetics. 2001 Feb;157(2):503-18. PMID:11156974
- ↑ Jaspersen SL, Giddings TH Jr, Winey M. Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p. J Cell Biol. 2002 Dec 23;159(6):945-56. Epub 2002 Dec 16. PMID:12486115 doi:http://dx.doi.org/10.1083/jcb.200208169
- ↑ Kilmartin JV. Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication. J Cell Biol. 2003 Sep 29;162(7):1211-21. Epub 2003 Sep 22. PMID:14504268 doi:http://dx.doi.org/10.1083/jcb.200307064
- ↑ Ma P, Winderickx J, Nauwelaers D, Dumortier F, De Doncker A, Thevelein JM, Van Dijck P. Deletion of SFI1, a novel suppressor of partial Ras-cAMP pathway deficiency in the yeast Saccharomyces cerevisiae, causes G(2) arrest. Yeast. 1999 Aug;15(11):1097-109. PMID:10455233 doi:<1097::AID-YEA437>3.0.CO;2-B http://dx.doi.org/10.1002/(SICI)1097-0061(199908)15:11<1097::AID-YEA437>3.0.CO;2-B
- ↑ Kilmartin JV. Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication. J Cell Biol. 2003 Sep 29;162(7):1211-21. Epub 2003 Sep 22. PMID:14504268 doi:http://dx.doi.org/10.1083/jcb.200307064
- ↑ Li S, Sandercock AM, Conduit P, Robinson CV, Williams RL, Kilmartin JV. Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication. J Cell Biol. 2006 Jun 19;173(6):867-77. PMID:16785321 doi:10.1083/jcb.200603153
- ↑ Li S, Sandercock AM, Conduit P, Robinson CV, Williams RL, Kilmartin JV. Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication. J Cell Biol. 2006 Jun 19;173(6):867-77. PMID:16785321 doi:10.1083/jcb.200603153
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