4KOO

Crystal Structure of WHY1 from Arabidopsis thaliana

Summary for 4KOO

• Entry DOI: 10.2210/pdb4koo/pdb
• Related: 4KOP 4KOQ
• Descriptor: Single-stranded DNA-binding protein WHY1, chloroplastic, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, NICKEL (II) ION, ... (5 entities in total)
• Functional Keywords: plant, whirly, single-stranded dna binding protein, dna binding protein
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Plastid, chloroplast : Q9M9S3
• Total number of polymer chains: 4
• Total formula weight: 81356.69

Authors

Cappadocia, L.,Parent, J.S.,Brisson, N.,Sygusch, J. (deposition date: 2013-05-12, release date: 2013-11-13, Last modification date: 2024-02-28)

Primary citation

Cappadocia, L.,Parent, J.S.,Sygusch, J.,Brisson, N.
A family portrait: structural comparison of the Whirly proteins from Arabidopsis thaliana and Solanum tuberosum.
Acta Crystallogr.,Sect.F, 69:1207-1211, 2013

PubMed Abstract: 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.

PubMed: 24192350
DOI: 10.1107/S1744309113028698

Experimental method

X-RAY DIFFRACTION (1.88 Å)