7UJL

Bacteriophage Lambda Red-Beta N-terminal domain helical assembly in complex with dsDNA

7UJL の概要

• エントリーDOI: 10.2210/pdb7ujl/pdb
• EMDBエントリー: 26566
• 分子名称: Recombination protein bet, Template DNA, Complementary DNA (3 entities in total)
• 機能のキーワード: annealase, synaptase, ssap, single-strand annealing protein, dna annealing intermediate, recombinase, two-component recombinase, viral, dna-binding, recombination-dna complex, recombination/dna
• 由来する生物種: Escherichia virus Lambda; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 37870.69

構造登録者

Newing, T.P.,Tolun, G. (登録日: 2022-03-31, 公開日: 2022-10-05, 最終更新日: 2024-11-06)

主引用文献

Newing, T.P.,Brewster, J.L.,Fitschen, L.J.,Bouwer, J.C.,Johnston, N.P.,Yu, H.,Tolun, G.
Red beta 177 annealase structure reveals details of oligomerization and lambda Red-mediated homologous DNA recombination
Nat Commun, 13:5649-, 2022

PubMed Abstract: The Redβ protein of the bacteriophage λ red recombination system is a model annealase which catalyzes single-strand annealing homologous DNA recombination. Here we present the structure of a helical oligomeric annealing intermediate of Redβ, consisting of N-terminal residues 1-177 bound to two complementary 27mer oligonucleotides, determined via cryogenic electron microscopy (cryo-EM) to a final resolution of 3.3 Å. The structure reveals a continuous binding groove which positions and stabilizes complementary DNA strands in a planar orientation to facilitate base pairing via a network of hydrogen bonding. Definition of the inter-subunit interface provides a structural basis for the propensity of Redβ to oligomerize into functionally significant long helical filaments, a trait shared by most annealases. Our cryo-EM structure and molecular dynamics simulations suggest that residues 133-138 form a flexible loop which modulates access to the binding groove. More than half a century after its discovery, this combination of structural and computational observations has allowed us to propose molecular mechanisms for the actions of the model annealase Redβ, a defining member of the Redβ/RecT protein family.

PubMed: 36163171
DOI: 10.1038/s41467-022-33090-6

実験手法

ELECTRON MICROSCOPY (3.3 Å)