5Z69

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

5Z69 の概要

• エントリーDOI: 10.2210/pdb5z69/pdb
• 分子名称: DNA replication and repair protein RecF, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER (3 entities in total)
• 機能のキーワード: recf, dna repair, recombination mediator, recfor, rad50, dna binding protein
• 由来する生物種: Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86912.71

構造登録者

Tang, Q.,Liu, Y.-P.,Yan, X.-X. (登録日: 2018-01-22, 公開日: 2018-10-17, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.102 Å)