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TitleRedβ annealase structure reveals details of oligomerization and λ Red-mediated homologous DNA recombination.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 5649, Year 2022
Publish dateSep 26, 2022
AuthorsTimothy P Newing / Jodi L Brewster / Lucy J Fitschen / James C Bouwer / Nikolas P Johnston / Haibo Yu / Gökhan Tolun /
PubMed AbstractThe 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 ...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.
External linksNat Commun / PubMed:36163171 / PubMed Central
MethodsEM (helical sym.)
Resolution3.3 Å
Structure data

26566

7ujl

EMDB-26566, PDB-7ujl:
Bacteriophage Lambda Red-Beta N-terminal domain helical assembly in complex with dsDNA
Method: EM (helical sym.) / Resolution: 3.3 Å

Source
  • escherichia virus lambda
  • escherichia coli (E. coli)
KeywordsRECOMBINATION/DNA / Annealase / Synaptase / SSAP / Single-strand annealing protein / DNA annealing intermediate / Recombinase / Two-component recombinase / Viral / DNA-binding / RECOMBINATION-DNA complex

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