5Z68

Structure of the recombination mediator protein RecF-ATP in RecFOR pathway

Summary for 5Z68

• Entry DOI: 10.2210/pdb5z68/pdb
• Descriptor: DNA replication and repair protein RecF, ADENOSINE-5'-TRIPHOSPHATE, IMIDAZOLE, ... (5 entities in total)
• Functional Keywords: recf, dna repair, recombination mediator, recfor, rad50, dna binding protein
• Biological source: Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis)
• Cellular location: Cytoplasm : Q8RDL3
• Total number of polymer chains: 4
• Total formula weight: 177136.65

Authors

Tang, Q.,Liu, Y.-P.,Yan, X.-X. (deposition date: 2018-01-22, release date: 2018-04-18, Last modification date: 2024-10-23)

Primary citation

Tang, Q.,Liu, Y.P.,Shan, H.H.,Tian, L.F.,Zhang, J.Z.,Yan, X.X.
ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair.
Sci Rep, 8:2127-2127, 2018

PubMed Abstract: RecF is a principal member of the RecF pathway. It interacts with RecO and RecR to initiate homologous recombination by loading RecA recombinases on single-stranded DNA and displacing single-stranded DNA-binding proteins. As an ATP-binding cassette ATPase, RecF exhibits ATP-dependent dimerization and structural homology with Rad50 and SMC proteins. However, the mechanism and action pattern of RecF ATP-dependent dimerization remains unclear. Here, We determined three crystal structures of TTERecF, TTERecF-ATP and TTERecF-ATPɤS from Thermoanaerobacter tengcongensis that reveal a novel ATP-driven RecF dimerization. RecF contains a positively charged tunnel on its dimer interface that is essential to ATP binding. Our structural and biochemical data indicate that the Walker A motif serves as a switch and plays a key role in ATP binding and RecF dimerization. Furthermore, Biolayer interferometry assay results showed that the TTERecF interacted with ATP and formed a dimer, displaying a higher affinity for DNA than that of the TTERecF monomer. Overall, our results provide a solid structural basis for understanding the process of RecF binding with ATP and the functional mechanism of ATP-dependent RecF dimerization.

PubMed: 29391496
DOI: 10.1038/s41598-018-20557-0

Experimental method

X-RAY DIFFRACTION (3 Å)