7UJL
Bacteriophage Lambda Red-Beta N-terminal domain helical assembly in complex with dsDNA
Summary for 7UJL
| Entry DOI | 10.2210/pdb7ujl/pdb |
| EMDB information | 26566 |
| Descriptor | Recombination protein bet, Template DNA, Complementary DNA (3 entities in total) |
| Functional Keywords | annealase, synaptase, ssap, single-strand annealing protein, dna annealing intermediate, recombinase, two-component recombinase, viral, dna-binding, recombination-dna complex, recombination/dna |
| Biological source | Escherichia virus Lambda More |
| Total number of polymer chains | 3 |
| Total formula weight | 37870.69 |
| Authors | Newing, T.P.,Tolun, G. (deposition date: 2022-03-31, release date: 2022-10-05, Last modification date: 2024-11-06) |
| Primary citation | 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 Cited by 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: 36163171DOI: 10.1038/s41467-022-33090-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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