4kop | pdb_00004kop
Crystal Structure of WHY2 from Arabidopsis thaliana
Structural highlights
FunctionWHY2_ARATH Single-stranded DNA-binding protein that associates with mitochondrial DNA and may play a role in the regulation of the gene expression machinery. Seems also to be required to prevent break-induced DNA rearrangements in the mitochondrial genome. Can bind to melt double-stranded DNA in vivo.[1] [2] [3] Publication Abstract from PubMedDNA 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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