2V1C

Crystal structure and mutational study of RecOR provide insight into its role in DNA repair

2V1C の概要

• エントリーDOI: 10.2210/pdb2v1c/pdb
• 関連するPDBエントリー: 1U5K 1VDD 1W3S
• 分子名称: RECOMBINATION PROTEIN RECR, HYPOTHETICAL PROTEIN, ZINC ION (3 entities in total)
• 機能のキーワード: recombination, homologous recombination, recfor pathway, dna recombination, dna binding, zinc-finger, metal-binding, recor complex, hypothetical protein, deinococcus radiodurans, recr, zinc, reco, dna damage, dna repair
• 由来する生物種: DEINOCOCCUS RADIODURANS; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 74077.03

構造登録者

Timmins, J.,Leiros, I.,McSweeney, S. (登録日: 2007-05-23, 公開日: 2007-07-03, 最終更新日: 2023-12-13)

主引用文献

Timmins, J.,Leiros, I.,Mcsweeney, S.
Crystal Structure and Mutational Study of Recor Provide Insight Into its Mode of DNA Binding.
Embo J., 26:3260-, 2007

PubMed Abstract: The crystal structure of the complex formed between Deinococcus radiodurans RecR and RecO (drRecOR) has been determined. In accordance with previous biochemical characterisation, the drRecOR complex displays a RecR:RecO molecular ratio of 2:1. The biologically relevant drRecOR entity consists of a heterohexamer in the form of two drRecO molecules positioned on either side of the tetrameric ring of drRecR, with their OB (oligonucleotide/oligosaccharide-binding) domains pointing towards the interior of the ring. Mutagenesis studies validated the protein-protein interactions observed in the crystal structure and allowed mapping of the residues in the drRecOR complex required for DNA binding. Furthermore, the preferred DNA substrate of drRecOR was identified as being 3'-overhanging DNA, as encountered at ssDNA-dsDNA junctions. Together these results suggest a possible mechanism for drRecOR recognition of stalled replication forks.

PubMed: 17581636
DOI: 10.1038/SJ.EMBOJ.7601760

実験手法

X-RAY DIFFRACTION (3.8 Å)