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

ABSTRACT:

SUBMITTER: Charles E Bell

PROVIDER: EMPIAR-11348 | biostudies-other |

REPOSITORIES: biostudies-other

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Structure of a RecT/Redβ family recombinase in complex with a duplex intermediate of DNA annealing.

Caldwell Brian J BJ Norris Andrew S AS Karbowski Caroline F CF Wiegand Alyssa M AM Wysocki Vicki H VH Bell Charles E CE

Nature communications 20221221 1

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 h ...[more]

PMID: 36543802

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Structure of RecT protein from Listeria innoccua phage A118 in complex with 83-mer single stranded DNA

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