6T8B

FtsK motor domain with dsDNA, translocating state

6T8B の概要

• エントリーDOI: 10.2210/pdb6t8b/pdb
• 関連するPDBエントリー: 6T8G 6T8O
• EMDBエントリー: 10399
• 分子名称: DNA translocase FtsK, dsDNA substrate, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• 機能のキーワード: dna translocation, dna motor, reca fold, divisome, dna binding protein
• 由来する生物種: Pseudomonas aeruginosa PAO1; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 339215.29

構造登録者

Jean, N.L.,Lowe, J. (登録日: 2019-10-24, 公開日: 2019-11-20, 最終更新日: 2024-05-22)

主引用文献

Jean, N.L.,Rutherford, T.J.,Lowe, J.
FtsK in motion reveals its mechanism for double-stranded DNA translocation.
Proc.Natl.Acad.Sci.USA, 117:14202-14208, 2020

PubMed Abstract: FtsK protein contains a fast DNA motor that is involved in bacterial chromosome dimer resolution. During cell division, FtsK translocates double-stranded DNA until both recombination sites are placed at mid cell for subsequent dimer resolution. Here, we solved the 3.6-Å resolution electron cryo-microscopy structure of the motor domain of FtsK while translocating on its DNA substrate. Each subunit of the homo-hexameric ring adopts a unique conformation and one of three nucleotide states. Two DNA-binding loops within four subunits form a pair of spiral staircases within the ring, interacting with the two DNA strands. This suggests that simultaneous conformational changes in all ATPase domains at each catalytic step generate movement through a mechanism related to filament treadmilling. While the ring is only rotating around the DNA slowly, it is instead the conformational states that rotate around the ring as the DNA substrate is pushed through.

PubMed: 32513722
DOI: 10.1073/pnas.2001324117

実験手法

ELECTRON MICROSCOPY (3.65 Å)