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RedBeta177 oligomeric helical assembly bound to two complementary 27mer ssDNA oligonucleotides


ABSTRACT:

SUBMITTER: Gökhan Tolun 

PROVIDER: EMPIAR-11262 | biostudies-other |

REPOSITORIES: biostudies-other

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Redβ<sub>177</sub> annealase structure reveals details of oligomerization and λ Red-mediated homologous DNA recombination.

Newing Timothy P TP   Brewster Jodi L JL   Fitschen Lucy J LJ   Bouwer James C JC   Johnston Nikolas P NP   Yu Haibo H   Tolun Gökhan G  

Nature communications 20220926 1


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  ...[more]

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