5DCF

C-terminal domain of XerD recombinase in complex with gamma domain of FtsK

5DCF の概要

• エントリーDOI: 10.2210/pdb5dcf/pdb
• 分子名称: Tyrosine recombinase XerD,DNA translocase FtsK (2 entities in total)
• 機能のキーワード: recombination
• 由来する生物種: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30725.85

構造登録者

Keller, A.N.,Xin, Y.,Lowe, J.,Grainge, I. (登録日: 2015-08-24, 公開日: 2016-09-07, 最終更新日: 2023-09-27)

主引用文献

Keller, A.N.,Xin, Y.,Boer, S.,Reinhardt, J.,Baker, R.,Arciszewska, L.K.,Lewis, P.J.,Sherratt, D.J.,Lowe, J.,Grainge, I.
Activation of Xer-recombination at dif: structural basis of the FtsK gamma-XerD interaction.
Sci Rep, 6:33357-33357, 2016

PubMed Abstract: Bacterial chromosomes are most often circular DNA molecules. This can produce a topological problem; a genetic crossover from homologous recombination results in dimerization of the chromosome. A chromosome dimer is lethal unless resolved. A site-specific recombination system catalyses this dimer-resolution reaction at the chromosomal site dif. In Escherichia coli, two tyrosine-family recombinases, XerC and XerD, bind to dif and carry out two pairs of sequential strand exchange reactions. However, what makes the reaction unique among site-specific recombination reactions is that the first step, XerD-mediated strand exchange, relies on interaction with the very C-terminus of the FtsK DNA translocase. FtsK is a powerful molecular motor that functions in cell division, co-ordinating division with clearing chromosomal DNA from the site of septation and also acts to position the dif sites for recombination. This is a model system for unlinking, separating and segregating large DNA molecules. Here we describe the molecular detail of the interaction between XerD and FtsK that leads to activation of recombination as deduced from a co-crystal structure, biochemical and in vivo experiments. FtsKγ interacts with the C-terminal domain of XerD, above a cleft where XerC is thought to bind. We present a model for activation of recombination based on structural data.

PubMed: 27708355
DOI: 10.1038/srep33357

実験手法

X-RAY DIFFRACTION (2.3 Å)