1U5K

Recombinational repair protein RecO

Summary for 1U5K

• Entry DOI: 10.2210/pdb1u5k/pdb
• Descriptor: hypothetical protein, ZINC ION (3 entities in total)
• Functional Keywords: obd-fold, zn-binding, recombination, replication
• Biological source: Deinococcus radiodurans
• Total number of polymer chains: 2
• Total formula weight: 52883.70

Authors

Makharashvili, N.,Koroleva, O.,Bera, S.,Grandgenett, D.P.,Korolev, S. (deposition date: 2004-07-27, release date: 2004-10-26, Last modification date: 2024-02-14)

Primary citation

Makharashvili, N.,Koroleva, O.,Bera, S.,Grandgenett, D.P.,Korolev, S.
A Novel Structure of DNA Repair Protein RecO from Deinococcus radiodurans
STRUCTURE, 12:1881-1889, 2004

PubMed Abstract: Recovery of arrested replication requires coordinated action of DNA repair, replication, and recombination machineries. Bacterial RecO protein is a member of RecF recombination repair pathway important for replication recovery. RecO possesses two distinct activities in vitro, closely resembling those of eukaryotic protein Rad52: DNA annealing and RecA-mediated DNA recombination. Here we present the crystal structure of the RecO protein from the extremely radiation resistant bacteria Deinococcus radiodurans (DrRecO) and characterize its DNA binding and strand annealing properties. The RecO structure is totally different from the Rad52 structure. DrRecO is comprised of three structural domains: an N-terminal domain which adopts an OB-fold, a novel alpha-helical domain, and an unusual zinc-binding domain. Sequence alignments suggest that the multidomain architecture is conserved between RecO proteins from other bacterial species and is suitable to elucidate sites of protein-protein and DNA-protein interactions necessary for RecO functions during the replication recovery and DNA repair.

PubMed: 15458636
DOI: 10.1016/j.str.2004.08.006

Experimental method

X-RAY DIFFRACTION (2 Å)