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TitleThe LexA-RecA* structure reveals a cryptic lock-and-key mechanism for SOS activation.
Journal, issue, pagesNat Struct Mol Biol, Year 2024
Publish dateMay 16, 2024
AuthorsMichael B Cory / Allen Li / Christina M Hurley / Peter J Carman / Ruth A Pumroy / Zachary M Hostetler / Ryann M Perez / Yarra Venkatesh / Xinning Li / Kushol Gupta / E James Petersson / Rahul M Kohli /
PubMed AbstractThe bacterial SOS response plays a key role in adaptation to DNA damage, including genomic stress caused by antibiotics. SOS induction begins when activated RecA*, an oligomeric nucleoprotein ...The bacterial SOS response plays a key role in adaptation to DNA damage, including genomic stress caused by antibiotics. SOS induction begins when activated RecA*, an oligomeric nucleoprotein filament that forms on single-stranded DNA, binds to and stimulates autoproteolysis of the repressor LexA. Here, we present the structure of the complete Escherichia coli SOS signal complex, constituting full-length LexA bound to RecA*. We uncover an extensive interface unexpectedly including the LexA DNA-binding domain, providing a new molecular rationale for ordered SOS gene induction. We further find that the interface involves three RecA subunits, with a single residue in the central engaged subunit acting as a molecular key, inserting into an allosteric binding pocket to induce LexA cleavage. Given the pro-mutagenic nature of SOS activation, our structural and mechanistic insights provide a foundation for developing new therapeutics to slow the evolution of antibiotic resistance.
External linksNat Struct Mol Biol / PubMed:38755298
MethodsEM (helical sym.)
Resolution2.93 Å
Structure data

41579

8trg

EMDB-41579, PDB-8trg:
Structure of full-length LexA bound to a RecA filament
Method: EM (helical sym.) / Resolution: 2.93 Å

Chemicals

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsSIGNALING PROTEIN/DNA / Damage response / signal transduction / SIGNALING PROTEIN / SIGNALING PROTEIN-DNA complex

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