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| | ==Crystal Structure of WHY3 from Arabidopsis thaliana== | | ==Crystal Structure of WHY3 from Arabidopsis thaliana== |
| - | <StructureSection load='4koq' size='340' side='right' caption='[[4koq]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='4koq' size='340' side='right'caption='[[4koq]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4koq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KOQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4koq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KOQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4koo|4koo]], [[4kop|4kop]]</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=4koq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4koq OCA], [https://pdbe.org/4koq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4koq RCSB], [https://www.ebi.ac.uk/pdbsum/4koq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4koq ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At2g02740, PTAC11, T20F6.12, WHY3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=4koq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4koq OCA], [http://pdbe.org/4koq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4koq RCSB], [http://www.ebi.ac.uk/pdbsum/4koq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4koq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/WHY3_ARATH WHY3_ARATH]] Single-stranded DNA-binding protein that functions in both chloroplasts and nucleus. In chloroplasts, maintains plastid genome stability by preventing break-induced and short homology-dependent illegitimate recombinations. In the nucleus, is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Can bind double-stranded DNA in vivo.<ref>PMID:19669906</ref> <ref>PMID:19666500</ref> <ref>PMID:20551348</ref> <ref>PMID:21911368</ref> | + | [https://www.uniprot.org/uniprot/WHY3_ARATH WHY3_ARATH] Single-stranded DNA-binding protein that functions in both chloroplasts and nucleus. In chloroplasts, maintains plastid genome stability by preventing break-induced and short homology-dependent illegitimate recombinations. In the nucleus, is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Can bind double-stranded DNA in vivo.<ref>PMID:19669906</ref> <ref>PMID:19666500</ref> <ref>PMID:20551348</ref> <ref>PMID:21911368</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Brisson, N]] | + | [[Category: Large Structures]] |
| - | [[Category: Cappadocia, L]] | + | [[Category: Brisson N]] |
| - | [[Category: Parent, J S]] | + | [[Category: Cappadocia L]] |
| - | [[Category: Sygusch, J]] | + | [[Category: Parent JS]] |
| - | [[Category: Dna binding protein]]
| + | [[Category: Sygusch J]] |
| - | [[Category: Plant]]
| + | |
| - | [[Category: Single-stranded dna binding protein]]
| + | |
| - | [[Category: Whirly]]
| + | |
| Structural highlights
Function
WHY3_ARATH Single-stranded DNA-binding protein that functions in both chloroplasts and nucleus. In chloroplasts, maintains plastid genome stability by preventing break-induced and short homology-dependent illegitimate recombinations. In the nucleus, is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Can bind double-stranded DNA in vivo.[1] [2] [3] [4]
Publication Abstract from PubMed
DNA double-strand breaks are highly detrimental genomic lesions that routinely arise in genomes. To protect the integrity of their genetic information, all organisms have evolved specialized DNA-repair mechanisms. Whirly proteins modulate DNA repair in plant chloroplasts and mitochondria by binding single-stranded DNA in a non-sequence-specific manner. Although most of the results showing the involvement of the Whirly proteins in DNA repair have been obtained in Arabidopsis thaliana, only the crystal structures of the potato Whirly proteins WHY1 and WHY2 have been reported to date. The present report of the crystal structures of the three Whirly proteins from A. thaliana (WHY1, WHY2 and WHY3) reveals that these structurally similar proteins assemble into tetramers. Furthermore, structural alignment with a potato WHY2-DNA complex reveals that the residues in these proteins are properly oriented to bind single-stranded DNA in a non-sequence-specific manner.
A family portrait: structural comparison of the Whirly proteins from Arabidopsis thaliana and Solanum tuberosum.,Cappadocia L, Parent JS, Sygusch J, Brisson N Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1207-11., doi: 10.1107/S1744309113028698. Epub 2013 Oct 26. PMID:24192350[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xiong JY, Lai CX, Qu Z, Yang XY, Qin XH, Liu GQ. Recruitment of AtWHY1 and AtWHY3 by a distal element upstream of the kinesin gene AtKP1 to mediate transcriptional repression. Plant Mol Biol. 2009 Nov;71(4-5):437-49. doi: 10.1007/s11103-009-9533-7. Epub, 2009 Aug 11. PMID:19669906 doi:http://dx.doi.org/10.1007/s11103-009-9533-7
- ↑ Marechal A, Parent JS, Veronneau-Lafortune F, Joyeux A, Lang BF, Brisson N. Whirly proteins maintain plastid genome stability in Arabidopsis. Proc Natl Acad Sci U S A. 2009 Aug 25;106(34):14693-8. doi:, 10.1073/pnas.0901710106. Epub 2009 Aug 7. PMID:19666500 doi:http://dx.doi.org/10.1073/pnas.0901710106
- ↑ Cappadocia L, Marechal A, Parent JS, Lepage E, Sygusch J, Brisson N. Crystal structures of DNA-Whirly complexes and their role in Arabidopsis organelle genome repair. Plant Cell. 2010 Jun;22(6):1849-67. Epub 2010 Jun 15. PMID:20551348 doi:10.1105/tpc.109.071399
- ↑ Cappadocia L, Parent JS, Zampini E, Lepage E, Sygusch J, Brisson N. A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage. Nucleic Acids Res. 2011 Sep 12. PMID:21911368 doi:10.1093/nar/gkr740
- ↑ Cappadocia L, Parent JS, Sygusch J, Brisson N. A family portrait: structural comparison of the Whirly proteins from Arabidopsis thaliana and Solanum tuberosum. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1207-11., doi: 10.1107/S1744309113028698. Epub 2013 Oct 26. PMID:24192350 doi:http://dx.doi.org/10.1107/S1744309113028698
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