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- W2022197835 abstract "The key event in the switch from lysogenic to lytic growth of phage lambda is the self-cleavage of lambda repressor, which is induced by the formation of a RecA-ssDNA-ATP filament at a site of DNA damage. Lambda repressor cleaves itself at the peptide bond between Ala111 and Gly112, but only when bound as a monomer to the RecA-ssDNA-ATP filament. Here we have designed a hyper-cleavable fragment of lambda repressor containing the hinge and C-terminal domain (residues 101–229), in which the monomer–monomer interface is disrupted by two point mutations and a deletion of seven residues at the C terminus. This fragment crystallizes as a monomer and its structure has been determined to 1.8 Å resolution. The hinge region, which bears the cleavage site, is folded over the active site of the C-terminal oligomerization domain (CTD) but with the cleavage site flipped out and exposed to solvent. Thus, the structure represents a non-cleavable conformation of the repressor, but one that is poised for cleavage after modest rearrangements that are presumably stabilized by binding to RecA. The structure provides a unique snapshot of lambda repressor in a conformation that sheds light on how its self-cleavage is tempered in the absence of RecA, as well as a framework for interpreting previous genetic and biochemical data concerning the RecA-mediated cleavage reaction." @default.
- W2022197835 created "2016-06-24" @default.
- W2022197835 creator A5067691635 @default.
- W2022197835 creator A5074019511 @default.
- W2022197835 date "2006-09-01" @default.
- W2022197835 modified "2023-09-27" @default.
- W2022197835 title "Structure of a Hyper-cleavable Monomeric Fragment of Phage λ Repressor Containing the Cleavage Site Region" @default.
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- W2022197835 doi "https://doi.org/10.1016/j.jmb.2006.07.026" @default.
- W2022197835 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1896146" @default.
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