8RXT

ComM helicase hexamer in abscence o DNA

8RXT の概要

• エントリーDOI: 10.2210/pdb8rxt/pdb
• EMDBエントリー: 19573 19574 19575 19577 19578 19579
• 分子名称: Competence related protein ComM, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (2 entities in total)
• 機能のキーワード: helicase, translocase, natural transformation, dna binding protein
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 337120.52

構造登録者

Talachia Rosa, L.,Fronzes, R. (登録日: 2024-02-07, 公開日: 2024-10-30, 最終更新日: 2025-07-09)

主引用文献

Rosa, L.T.,Vernhes, E.,Soulet, A.L.,Polard, P.,Fronzes, R.
Structural insights into the mechanism of DNA branch migration during homologous recombination in bacteria.
Embo J., 43:6180-6198, 2024

PubMed Abstract: Some DNA helicases play central and specific roles in genome maintenance and plasticity through their branch migration activity in different pathways of homologous recombination. RadA is a highly conserved bacterial helicase involved in DNA repair throughout all bacterial species. In Gram-positive Firmicutes, it also has a role in natural transformation, while in Gram-negative bacteria, ComM is the canonical transformation-specific helicase. Both RadA and ComM helicases form hexameric rings and use ATP hydrolysis as an energy source to propel themselves along DNA. In this study, we present the cryoEM structures of RadA and ComM interacting with DNA and ATP analogs. These structures reveal important molecular interactions that couple ATP hydrolysis and DNA binding in RadA, as well as the role of the Lon protease-like domain, shared by RadA and ComM, in this process. Taken together, these results provide new molecular insights into the mechanisms of DNA branch migration in different pathways of homologous recombination.

PubMed: 39424952
DOI: 10.1038/s44318-024-00264-5

実験手法

ELECTRON MICROSCOPY (3.93 Å)