1W3S

The crystal structure of RecO from Deinococcus radiodurans.

Summary for 1W3S

• Entry DOI: 10.2210/pdb1w3s/pdb
• Related: 1U5K
• Descriptor: HYPOTHETICAL PROTEIN DR0819, ZINC ION (3 entities in total)
• Functional Keywords: dna repair, sad, cys4 zinc finger, ob-fold, reco
• Biological source: DEINOCOCCUS RADIODURANS
• Total number of polymer chains: 2
• Total formula weight: 52883.70

Authors

Leiros, I.,Timmins, J.,Hall, D.R.,Leonard, G.A.,McSweeney, S.M. (deposition date: 2004-07-18, release date: 2005-02-23, Last modification date: 2024-05-08)

Primary citation

Leiros, I.,Timmins, J.,Hall, D.R.,Mcsweeney, S.M.
Crystal Structure and DNA-Binding Analysis of Reco from Deinococcus Radiodurans
Embo J., 24:906-, 2005

PubMed Abstract: The RecFOR pathway has been shown to be essential for DNA repair through the process of homologous recombination in bacteria and, recently, to be important in the recovery of stalled replication forks following UV irradiation. RecO, along with RecR, RecF, RecQ and RecJ, is a principal actor in this fundamental DNA repair pathway. Here we present the three-dimensional structure of a member of the RecO family. The crystal structure of Deinococcus radiodurans RecO (drRecO) reveals possible binding sites for DNA and for the RecO-binding proteins within its three discrete structural regions: an N-terminal oligonucleotide/oligosaccharide-binding domain, a helical bundle and a zinc-finger motif. Furthermore, drRecO was found to form a stable complex with RecR and to bind both single- and double-stranded DNA. Mutational analysis confirmed the existence of multiple DNA-binding sites within the protein.

PubMed: 15719017
DOI: 10.1038/SJ.EMBOJ.7600582

Experimental method

X-RAY DIFFRACTION (2.4 Å)