Structural highlights
Function
[RECR_DEIRA] May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO (By similarity). [Q9RW50_DEIRA] Involved in DNA repair and RecF pathway recombination (By similarity).[HAMAP-Rule:MF_00201][SAAS:SAAS022572_004_002906]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding.,Timmins J, Leiros I, McSweeney S EMBO J. 2007 Jul 11;26(13):3260-71. Epub 2007 Jun 21. PMID:17581636[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Timmins J, Leiros I, McSweeney S. Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding. EMBO J. 2007 Jul 11;26(13):3260-71. Epub 2007 Jun 21. PMID:17581636
