2V1C

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

Summary for 2V1C

• Entry DOI: 10.2210/pdb2v1c/pdb
• Related: 1U5K 1VDD 1W3S
• Descriptor: RECOMBINATION PROTEIN RECR, HYPOTHETICAL PROTEIN, ZINC ION (3 entities in total)
• Functional Keywords: 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
• Biological source: DEINOCOCCUS RADIODURANS; More
• Total number of polymer chains: 3
• Total formula weight: 74077.03

Authors

Timmins, J.,Leiros, I.,McSweeney, S. (deposition date: 2007-05-23, release date: 2007-07-03, Last modification date: 2023-12-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.8 Å)