5Z2V

Crystal structure of RecR from Pseudomonas aeruginosa PAO1

Summary for 5Z2V

• Entry DOI: 10.2210/pdb5z2v/pdb
• Descriptor: Recombination protein RecR, ZINC ION, GLYCEROL, ... (7 entities in total)
• Functional Keywords: recr dna binding homologous recombination, dna binding protein
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• Total number of polymer chains: 2
• Total formula weight: 43043.92

Authors

Che, S.,Zhang, Q.,Bartlam, M. (deposition date: 2018-01-04, release date: 2019-01-02, Last modification date: 2023-11-22)

Primary citation

Che, S.,Chen, Y.,Liang, Y.,Zhang, Q.,Bartlam, M.
Crystal structure of RecR, a member of the RecFOR DNA-repair pathway, from Pseudomonas aeruginosa PAO1.
Acta Crystallogr F Struct Biol Commun, 74:222-230, 2018

PubMed Abstract: DNA damage is usually lethal to all organisms. Homologous recombination plays an important role in the DNA damage-repair process in prokaryotic organisms. Two pathways are responsible for homologous recombination in Pseudomonas aeruginosa: the RecBCD pathway and the RecFOR pathway. RecR is an important regulator in the RecFOR homologous recombination pathway in P. aeruginosa. It forms complexes with RecF and RecO that can facilitate the loading of RecA onto ssDNA in the RecFOR pathway. Here, the crystal structure of RecR from P. aeruginosa PAO1 (PaRecR) is reported. PaRecR crystallizes in space group P622, with two monomers per asymmetric unit. Analytical ultracentrifugation data show that PaRecR forms a stable dimer, but can exist as a tetramer in solution. The crystal structure shows that dimeric PaRecR forms a ring-like tetramer architecture via crystal symmetry. The presence of a ligand in the Walker B motif of one RecR subunit suggests a putative nucleotide-binding site.

PubMed: 29633970
DOI: 10.1107/S2053230X18003503

Experimental method

X-RAY DIFFRACTION (2.2 Å)