2v1c
From Proteopedia
CRYSTAL STRUCTURE AND MUTATIONAL STUDY OF RECOR PROVIDE INSIGHT INTO ITS ROLE IN DNA REPAIR
Overview
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.
About this Structure
2V1C is a Protein complex structure of sequences from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 18:01:36 2008
Categories: Deinococcus radiodurans | Protein complex | Leiros, I. | Mcsweeney, S. | Timmins, J. | Deinococcus radioduran | Dna binding | Dna damage | Dna recombination | Dna repair | Homologous recombination | Hypothetical protein | Metal-binding | Recfor pathway | Reco | Recombination | Recor complex | Recr | Zinc | Zinc-finger
