5Z67
Structure of the recombination mediator protein RecF in RecFOR pathway
5Z67 の概要
| エントリーDOI | 10.2210/pdb5z67/pdb |
| 分子名称 | DNA replication and repair protein RecF (2 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) |
| 細胞内の位置 | Cytoplasm : Q8RDL3 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 42511.04 |
| 構造登録者 | |
| 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 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: 29391496DOI: 10.1038/s41598-018-20557-0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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