2O5V

Recombination mediator RecF

Summary for 2O5V

• Entry DOI: 10.2210/pdb2o5v/pdb
• Descriptor: DNA replication and repair protein recF, SULFATE ION (3 entities in total)
• Functional Keywords: abc atpase, walker a motif, p-loop, signature motif, replication-recombination complex, replication/recombination
• Biological source: Deinococcus radiodurans
• Cellular location: Cytoplasm (By similarity): Q9RVE0
• Total number of polymer chains: 1
• Total formula weight: 39284.00

Authors

Korolev, S.,Koroleva, O. (deposition date: 2006-12-06, release date: 2007-02-06, Last modification date: 2023-12-27)

Primary citation

Koroleva, O.,Makharashvili, N.,Courcelle, C.T.,Courcelle, J.,Korolev, S.
Structural conservation of RecF and Rad50: implications for DNA recognition and RecF function.
Embo J., 26:867-877, 2007

PubMed Abstract: RecF, together with RecO and RecR, belongs to a ubiquitous group of recombination mediators (RMs) that includes eukaryotic proteins such as Rad52 and BRCA2. RMs help maintain genome stability in the presence of DNA damage by loading RecA-like recombinases and displacing single-stranded DNA-binding proteins. Here, we present the crystal structure of RecF from Deinococcus radiodurans. RecF exhibits a high degree of structural similarity with the head domain of Rad50, but lacks its long coiled-coil region. The structural homology between RecF and Rad50 is extensive, encompassing the ATPase subdomain and the so-called 'Lobe II' subdomain of Rad50. The pronounced structural conservation between bacterial RecF and evolutionarily diverged eukaryotic Rad50 implies a conserved mechanism of DNA binding and recognition of the boundaries of double-stranded DNA regions. The RecF structure, mutagenesis of conserved motifs and ATP-dependent dimerization of RecF are discussed with respect to its role in promoting presynaptic complex formation at DNA damage sites.

PubMed: 17255941
DOI: 10.1038/sj.emboj.7601537

Experimental method

X-RAY DIFFRACTION (1.61 Å)