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5Z67

Structure of the recombination mediator protein RecF in RecFOR pathway

Summary for 5Z67
Entry DOI10.2210/pdb5z67/pdb
DescriptorDNA replication and repair protein RecF (2 entities in total)
Functional Keywordsrecf, dna repair, recombination mediator, recfor, rad50, dna binding protein
Biological sourceCaldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis)
Cellular locationCytoplasm : Q8RDL3
Total number of polymer chains1
Total formula weight42511.04
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 citationTang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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