7UB2

Structure of RecT protein from Listeria innoccua phage A118 in complex with 83-mer annealed duplex

7UB2 の概要

• エントリーDOI: 10.2210/pdb7ub2/pdb
• EMDBエントリー: 26434
• 分子名称: RecT, DNA (49-mer) (3 entities in total)
• 機能のキーワード: dna recombination, dna annealing, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Listeria innocua Clip11262; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 339553.66

構造登録者

Bell, C.E.,Caldwell, B.J. (登録日: 2022-03-14, 公開日: 2022-12-07, 最終更新日: 2024-06-12)

主引用文献

Caldwell, B.J.,Norris, A.S.,Karbowski, C.F.,Wiegand, A.M.,Wysocki, V.H.,Bell, C.E.
Structure of a RecT/Red beta family recombinase in complex with a duplex intermediate of DNA annealing.
Nat Commun, 13:7855-7855, 2022

PubMed Abstract: Some bacteriophage encode a recombinase that catalyzes single-stranded DNA annealing (SSA). These proteins are apparently related to RAD52, the primary human SSA protein. The best studied protein, Redβ from bacteriophage λ, binds weakly to ssDNA, not at all to dsDNA, but tightly to a duplex intermediate of annealing formed when two complementary DNA strands are added to the protein sequentially. We used single particle cryo-electron microscopy (cryo-EM) to determine a 3.4 Å structure of a Redβ homolog from a prophage of Listeria innocua in complex with two complementary 83mer oligonucleotides. The structure reveals a helical protein filament bound to a DNA duplex that is highly extended and unwound. Native mass spectrometry confirms that the complex seen by cryo-EM is the predominant species in solution. The protein shares a common core fold with RAD52 and a similar mode of ssDNA-binding. These data provide insights into the mechanism of protein-catalyzed SSA.

PubMed: 36543802
DOI: 10.1038/s41467-022-35572-z

実験手法

ELECTRON MICROSCOPY (3.4 Å)