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| | ==Crystal structure of Swi5-Sfr1 complex from fission yeast== | | ==Crystal structure of Swi5-Sfr1 complex from fission yeast== |
| - | <StructureSection load='3viq' size='340' side='right' caption='[[3viq]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='3viq' size='340' side='right'caption='[[3viq]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3viq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VIQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3viq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VIQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vir|3vir]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vir|3vir]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sfr1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), swi5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sfr1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast]), swi5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=3viq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3viq OCA], [http://pdbe.org/3viq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3viq RCSB], [http://www.ebi.ac.uk/pdbsum/3viq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3viq 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=3viq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3viq OCA], [https://pdbe.org/3viq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3viq RCSB], [https://www.ebi.ac.uk/pdbsum/3viq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3viq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SFR1_SCHPO SFR1_SCHPO]] Involved in DNA recombination repair and meiotic chromosome segregation.<ref>PMID:14663140</ref> <ref>PMID:16303567</ref> [[http://www.uniprot.org/uniprot/SWI5_SCHPO SWI5_SCHPO]] Required for normal mating-type switching. Also involved in the rhp51-dependent recombination DNA repair pathway.<ref>PMID:14663140</ref> | + | [[https://www.uniprot.org/uniprot/SFR1_SCHPO SFR1_SCHPO]] Involved in DNA recombination repair and meiotic chromosome segregation.<ref>PMID:14663140</ref> <ref>PMID:16303567</ref> [[https://www.uniprot.org/uniprot/SWI5_SCHPO SWI5_SCHPO]] Required for normal mating-type switching. Also involved in the rhp51-dependent recombination DNA repair pathway.<ref>PMID:14663140</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Fission yeast]] | | [[Category: Fission yeast]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Hashimoto, H]] | | [[Category: Hashimoto, H]] |
| | [[Category: Ikeguchi, M]] | | [[Category: Ikeguchi, M]] |
| Structural highlights
Function
[SFR1_SCHPO] Involved in DNA recombination repair and meiotic chromosome segregation.[1] [2] [SWI5_SCHPO] Required for normal mating-type switching. Also involved in the rhp51-dependent recombination DNA repair pathway.[3]
Publication Abstract from PubMed
Rad51 forms a helical filament on single-stranded DNA and promotes strand exchange between two homologous DNA molecules during homologous recombination. The Swi5-Sfr1 complex interacts directly with Rad51 and stimulates strand exchange. Here we describe structural and functional aspects of the complex. Swi5 and the C-terminal core domain of Sfr1 form an essential activator complex with a parallel coiled-coil heterodimer joined firmly together via two previously uncharacterized leucine-zipper motifs and a bundle. The resultant coiled coil is sharply kinked, generating an elongated crescent-shaped structure suitable for transient binding within the helical groove of the Rad51 filament. The N-terminal region of Sfr1, meanwhile, has an interface for binding of Rad51. Our data suggest that the snug fit resulting from the complementary geometry of the heterodimer activates the Rad51 filament and that the N-terminal domain of Sfr1 plays a role in the efficient recruitment of the Swi5-Sfr1 complex to the Rad51 filaments.
Mechanistic insights into the activation of Rad51-mediated strand exchange from the structure of a recombination activator, the Swi5-Sfr1 complex.,Kuwabara N, Murayama Y, Hashimoto H, Kokabu Y, Ikeguchi M, Sato M, Mayanagi K, Tsutsui Y, Iwasaki H, Shimizu T Structure. 2012 Mar 7;20(3):440-9. PMID:22405003[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Akamatsu Y, Dziadkowiec D, Ikeguchi M, Shinagawa H, Iwasaki H. Two different Swi5-containing protein complexes are involved in mating-type switching and recombination repair in fission yeast. Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15770-5. Epub 2003 Dec 8. PMID:14663140 doi:http://dx.doi.org/10.1073/pnas.2632890100
- ↑ Martin-Castellanos C, Blanco M, Rozalen AE, Perez-Hidalgo L, Garcia AI, Conde F, Mata J, Ellermeier C, Davis L, San-Segundo P, Smith GR, Moreno S. A large-scale screen in S. pombe identifies seven novel genes required for critical meiotic events. Curr Biol. 2005 Nov 22;15(22):2056-62. PMID:16303567 doi:http://dx.doi.org/S0960-9822(05)01277-7
- ↑ Akamatsu Y, Dziadkowiec D, Ikeguchi M, Shinagawa H, Iwasaki H. Two different Swi5-containing protein complexes are involved in mating-type switching and recombination repair in fission yeast. Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15770-5. Epub 2003 Dec 8. PMID:14663140 doi:http://dx.doi.org/10.1073/pnas.2632890100
- ↑ Kuwabara N, Murayama Y, Hashimoto H, Kokabu Y, Ikeguchi M, Sato M, Mayanagi K, Tsutsui Y, Iwasaki H, Shimizu T. Mechanistic insights into the activation of Rad51-mediated strand exchange from the structure of a recombination activator, the Swi5-Sfr1 complex. Structure. 2012 Mar 7;20(3):440-9. PMID:22405003 doi:10.1016/j.str.2012.01.005
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