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5Z67

Structure of the recombination mediator protein RecF in RecFOR pathway

5Z67 の概要
エントリーDOI10.2210/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
Tang, Q.,Liu, Y.-P.,Yan, X.-X. (登録日: 2018-01-22, 公開日: 2018-04-18, 最終更新日: 2024-10-23)
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: 29391496
DOI: 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)
構造検証レポート
Validation report summary of 5z67
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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