5LD2

Cryo-EM structure of RecBCD+DNA complex revealing activated nuclease domain

5LD2 の概要

• エントリーDOI: 10.2210/pdb5ld2/pdb
• EMDBエントリー: 4038
• 分子名称: RecBCD enzyme subunit RecB,RecBCD enzyme subunit RecB,RecBCD enzyme subunit RecB, RecBCD enzyme subunit RecC, RecBCD enzyme subunit RecD, ... (6 entities in total)
• 機能のキーワード: helicase, nuclease, sh3, homologous recombination, hydrolase
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 351710.12

構造登録者

Wilkinson, M.,Chaban, Y.,Wigley, D.B. (登録日: 2016-06-23, 公開日: 2016-10-05, 最終更新日: 2024-05-15)

主引用文献

Wilkinson, M.,Chaban, Y.,Wigley, D.B.
Mechanism for nuclease regulation in RecBCD.
Elife, 5:-, 2016

PubMed Abstract: In bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is catalysed by AddAB, AdnAB or RecBCD-type helicase-nucleases. These enzyme complexes are highly processive, duplex unwinding and degrading machines that require tight regulation. Here, we report the structure of E.coli RecBCD, determined by cryoEM at 3.8 Å resolution, with a DNA substrate that reveals how the nuclease activity of the complex is activated once unwinding progresses. Extension of the 5'-tail of the unwound duplex induces a large conformational change in the RecD subunit, that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit. The process involves a SH3 domain that binds to a region of the RecB subunit in a binding mode that is distinct from others observed previously in SH3 domains and, to our knowledge, this is the first example of peptide-binding of an SH3 domain in a bacterial system.

PubMed: 27644322
DOI: 10.7554/eLife.18227

実験手法

ELECTRON MICROSCOPY (3.83 Å)