4koq

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m (Protected "4koq" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4koq| PDB=4koq | SCENE= }}
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===Crystal Structure of WHY3 from Arabidopsis thaliana===
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The entry 4koq is ON HOLD until Paper Publication
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==Function==
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[[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>
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Authors: Cappadocia, L., Parent, J.S., Brisson, N., Sygusch, J.
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==About this Structure==
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[[4koq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KOQ OCA].
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Description: Crystal Structure of WHY3 from Arabidopsis thaliana
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Brisson, N.]]
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[[Category: Cappadocia, L.]]
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[[Category: Parent, J S.]]
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[[Category: Sygusch, J.]]
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[[Category: Dna binding protein]]
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[[Category: Plant]]
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[[Category: Single-stranded dna binding protein]]
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[[Category: Whirly]]

Revision as of 08:29, 13 November 2013

Template:STRUCTURE 4koq

Contents

Crystal Structure of WHY3 from Arabidopsis thaliana

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]

About this Structure

4koq is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  1. 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
  2. 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
  3. 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
  4. 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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