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Literature summary for 3.4.21.88 extracted from

  • Butala, M.; Klose, D.; Hodnik, V.; Rems, A.; Podlesek, Z.; Klare, J.P.; Anderluh, G.; Busby, S.J.; Steinhoff, H.J.; Zgur-Bertok, D.
    Interconversion between bound and free conformations of LexA orchestrates the bacterial SOS response (2011), Nucleic Acids Res., 39, 6546-6557.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
RecA stimulates self-cleavage of a scissile peptide bond between Ala84 and Gly85, thereby de-activating LexA. Data indicate that the RecA filament predominately induces self-cleavage in one monomer of the LexA dimer and that the resulting LexA–LexA/CTD heterodimer is an inactive intermediate, exhibiting weaker DNA binding. RecA cannot induce self-cleavage in LexA that is bound to target DNA operator sites. In unbound LexA, the DNA-binding domains sample different conformations. One of these conformations is captured when LexA is bound to operator targets and this precludes interaction by RecA Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RecA stimulates self-cleavage of a scissile peptide bond between Ala84 and Gly85, thereby de-activating LexA. RecA cannot induce self-cleavage in LexA that is bound to target DNA operator sites. In unbound LexA, the DNA-binding domains sample different conformations. One of these conformations is captured when LexA is bound to operator targets and this precludes interaction by RecA. Hence, the conformational flexibility of unbound LexA is the key element in establishing a co-ordinated SOS response. While LexA exhibits diverse dissociation rates from operators, it interacts extremely rapidly with DNA target sites. Modulation of LexA activity changes the occurrence of persister cells in bacterial populations Escherichia coli ?
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