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| <StructureSection load='3ra0' size='340' side='right'caption='[[3ra0]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='3ra0' size='340' side='right'caption='[[3ra0]], [[Resolution|resolution]] 2.45Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3ra0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Potato Potato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RA0 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3ra0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RA0 FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r9y|3r9y]], [[3r9z|3r9z]], [[3n1h|3n1h]], [[3n1i|3n1i]], [[3n1j|3n1j]], [[3n1k|3n1k]], [[3n1l|3n1l]], [[1l3a|1l3a]]</div></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.451Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">StWhy2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4113 Potato])</td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ra0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ra0 OCA], [https://pdbe.org/3ra0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ra0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ra0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ra0 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=3ra0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ra0 OCA], [https://pdbe.org/3ra0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ra0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ra0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ra0 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[https://www.uniprot.org/uniprot/WHY2_SOLTU WHY2_SOLTU]] Single-stranded DNA-binding protein that may be involved in the maintenance of mitochondrial genome stability by preventing break-induced DNA rearrangements.<ref>PMID:21911368</ref>
| | [https://www.uniprot.org/uniprot/WHY2_SOLTU WHY2_SOLTU] Single-stranded DNA-binding protein that may be involved in the maintenance of mitochondrial genome stability by preventing break-induced DNA rearrangements.<ref>PMID:21911368</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| All organisms have evolved specialized DNA repair mechanisms in order to protect their genome against detrimental lesions such as DNA double-strand breaks. In plant organelles, these damages are repaired either through recombination or through a microhomology-mediated break-induced replication pathway. Whirly proteins are modulators of this second pathway in both chloroplasts and mitochondria. In this precise pathway, tetrameric Whirly proteins are believed to bind single-stranded DNA and prevent spurious annealing of resected DNA molecules with other regions in the genome. In this study, we add a new layer of complexity to this model by showing through atomic force microscopy that tetramers of the potato Whirly protein WHY2 further assemble into hexamers of tetramers, or 24-mers, upon binding long DNA molecules. This process depends on tetramer-tetramer interactions mediated by K67, a highly conserved residue among plant Whirly proteins. Mutation of this residue abolishes the formation of 24-mers without affecting the protein structure or the binding to short DNA molecules. Importantly, we show that an Arabidopsis Whirly protein mutated for this lysine is unable to rescue the sensitivity of a Whirly-less mutant plant to a DNA double-strand break inducing agent.
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| A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage.,Cappadocia L, Parent JS, Zampini E, Lepage E, Sygusch J, Brisson N Nucleic Acids Res. 2011 Sep 12. PMID:21911368<ref>PMID:21911368</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3ra0" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Potato]] | | [[Category: Solanum tuberosum]] |
| [[Category: Brisson, N]] | | [[Category: Brisson N]] |
| [[Category: Cappadocia, L]] | | [[Category: Cappadocia L]] |
| [[Category: Sygusch, J]] | | [[Category: Sygusch J]] |
| [[Category: Dna binding protein-dna complex]]
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| [[Category: Mitochondria]]
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| [[Category: Plant]]
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| [[Category: Protein-dna complex]]
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| [[Category: Single-stranded dna binding protein]]
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| [[Category: Stwhy2]]
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| [[Category: Whirly]]
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