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| - | {{STRUCTURE_4koo| PDB=4koo | SCENE= }} | |
| - | ===Crystal Structure of WHY1 from Arabidopsis thaliana=== | |
| - | {{ABSTRACT_PUBMED_24192350}} | |
| | | | |
| - | ==Function== | + | ==Crystal Structure of WHY1 from Arabidopsis thaliana== |
| - | [[http://www.uniprot.org/uniprot/WHY1_ARATH WHY1_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 nucleus, modulates telomere length homeostasis by inhibiting the action of the telomerase at the extreme termini of chromosomes. Is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Is required for full salicylic acid-dependent plant disease resistance responses. Can bind double-stranded DNA in vivo.<ref>PMID:14960277</ref> <ref>PMID:17217467</ref> <ref>PMID:19669906</ref> <ref>PMID:19666500</ref> <ref>PMID:20551348</ref> <ref>PMID:21911368</ref> | + | <StructureSection load='4koo' size='340' side='right'caption='[[4koo]], [[Resolution|resolution]] 1.88Å' scene=''> |
| - | | + | == Structural highlights == |
| - | ==About this Structure== | + | <table><tr><td colspan='2'>[[4koo]] is a 4 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=4KOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KOO FirstGlance]. <br> |
| - | [[4koo]] is a 4 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=4KOO OCA].
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88Å</td></tr> |
| - | | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | ==Reference==
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4koo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4koo OCA], [https://pdbe.org/4koo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4koo RCSB], [https://www.ebi.ac.uk/pdbsum/4koo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4koo ProSAT]</span></td></tr> |
| - | <ref group="xtra">PMID:024192350</ref><references group="xtra"/><references/>
| + | </table> |
| - | [[Category: Arath]] | + | == Function == |
| - | [[Category: Brisson, N.]] | + | [https://www.uniprot.org/uniprot/WHY1_ARATH WHY1_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 nucleus, modulates telomere length homeostasis by inhibiting the action of the telomerase at the extreme termini of chromosomes. Is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Is required for full salicylic acid-dependent plant disease resistance responses. Can bind double-stranded DNA in vivo.<ref>PMID:14960277</ref> <ref>PMID:17217467</ref> <ref>PMID:19669906</ref> <ref>PMID:19666500</ref> <ref>PMID:20551348</ref> <ref>PMID:21911368</ref> |
| - | [[Category: Cappadocia, L.]] | + | == References == |
| - | [[Category: Parent, J S.]] | + | <references/> |
| - | [[Category: Sygusch, J.]] | + | __TOC__ |
| - | [[Category: Dna binding protein]] | + | </StructureSection> |
| - | [[Category: Plant]]
| + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Single-stranded dna binding protein]]
| + | [[Category: Large Structures]] |
| - | [[Category: Whirly]]
| + | [[Category: Brisson N]] |
| | + | [[Category: Cappadocia L]] |
| | + | [[Category: Parent JS]] |
| | + | [[Category: Sygusch J]] |
| Structural highlights
Function
WHY1_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 nucleus, modulates telomere length homeostasis by inhibiting the action of the telomerase at the extreme termini of chromosomes. Is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Is required for full salicylic acid-dependent plant disease resistance responses. Can bind double-stranded DNA in vivo.[1] [2] [3] [4] [5] [6]
References
- ↑ Desveaux D, Subramaniam R, Despres C, Mess JN, Levesque C, Fobert PR, Dangl JL, Brisson N. A "Whirly" transcription factor is required for salicylic acid-dependent disease resistance in Arabidopsis. Dev Cell. 2004 Feb;6(2):229-40. PMID:14960277
- ↑ Yoo HH, Kwon C, Lee MM, Chung IK. Single-stranded DNA binding factor AtWHY1 modulates telomere length homeostasis in Arabidopsis. Plant J. 2007 Feb;49(3):442-51. Epub 2007 Jan 1. PMID:17217467 doi:http://dx.doi.org/10.1111/j.1365-313X.2006.02974.x
- ↑ 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
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