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2doq

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Revision as of 08:36, 12 October 2017

crystal structure of Sfi1p/Cdc31p complex

Structural highlights

2doq is a 4 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:	CDC31 (ATCC 18824), SFI1 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2doq"

@@ Line 1: / Line 1: @@
 ==crystal structure of Sfi1p/Cdc31p complex==
 <StructureSection load='2doq' size='340' side='right' caption='[[2doq]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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='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]</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=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>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 2doq" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Nucleoporin|Nucleoporin]]
 == References ==
 <references/>

2doq

From Proteopedia

Revision as of 08:36, 12 October 2017

crystal structure of Sfi1p/Cdc31p complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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