9F0Z

CryoEM structure of the F plasmid relaxosome with truncated TraI1-863 in its TE mode, derived from the ss-27_+8ds+9_+143-R_deltaAH+CTD Locally-refined 3.42 A Map

9F0Z の概要

• エントリーDOI: 10.2210/pdb9f0z/pdb
• EMDBエントリー: 50119
• 分子名称: T-strand DNA (96-MER), R-strand DNA (85-MER), Integration host factor subunit alpha, ... (7 entities in total)
• 機能のキーワード: relaxosome, bacterial conjugation, dna processing, relaxase, dna binding proteins, dna binding protein
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 257332.41

構造登録者

Williams, S.M.,Waksman, G. (登録日: 2024-04-17, 公開日: 2025-06-04, 最終更新日: 2025-07-09)

主引用文献

Williams, S.M.,Raffl, S.,Kienesberger, S.,Ilangovan, A.,Zechner, E.L.,Waksman, G.
Cryo-EM Structure of the relaxosome, a complex essential for bacterial mating and the spread of antibiotic resistance genes.
Nat Commun, 16:4906-4906, 2025

PubMed Abstract: Bacterial mating, or conjugation, was discovered nearly 80 years ago as a process transferring genes from one bacterial cell (the donor) to another (the recipient). It requires three key multiprotein complexes in the donor cell: a DNA-processing machinery called the relaxosome, a double-membrane spanning type 4 secretion system (T4SS), and an extracellular appendage termed pilus. While the near-atomic resolution structures of the T4SS and pilus are already known, that of the relaxosome has not been reported to date. Here, we describe the cryo-EM structure of the fully assembled relaxosome encoded by the paradigm F plasmid in two different states corresponding to distinct functional steps along the DNA processing reaction. By varying the structures of model DNAs we delineate conformational changes required to initiate conjugation. Mutational studies of the various protein-protein and protein-DNA interaction hubs suggest a complex sensitive to trigger signals, that could arise from cell-to-cell contacts with recipient cells.

PubMed: 40425557
DOI: 10.1038/s41467-025-60116-6

実験手法

ELECTRON MICROSCOPY (3.42 Å)