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- W4297239109 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." @default.
- W4297239109 created "2022-09-28" @default.
- W4297239109 creator A5015074981 @default.
- W4297239109 creator A5024535210 @default.
- W4297239109 creator A5045325196 @default.
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- W4297239109 creator A5065592363 @default.
- W4297239109 creator A5069025666 @default.
- W4297239109 creator A5072893058 @default.
- W4297239109 date "2022-09-26" @default.
- W4297239109 modified "2023-10-13" @default.
- W4297239109 title "Redβ177 annealase structure reveals details of oligomerization and λ Red-mediated homologous DNA recombination" @default.
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