bacterial and host-derived glutathione are required to activate prfa

bacterial and host-derived glutathione are required to activate prfa Allosteric GSH binding primes for DNA binding. (A B) C-di-AMP accumulation disrupts glutathione metabolism

Name: bacterial and host-derived glutathione are required to activate prfa Allosteric GSH binding primes for DNA binding. (A B) C-di-AMP accumulation disrupts glutathione metabolism
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C di AMP accumulation disrupts glutathione metabolism in Listeria monocytogenes Infection and Immunity Streptococcus pyogenes Hijacks Host Glutathione for Growth and Innate Immune Evasion mBio RCSB PDB 5LRS: The Transcriptional Regulator PrfA from Listeria Monocytogenes in complex with glutathione and a 30 bp operator PrfA box motif Diverse roles of low molecular weight thiol GSH in Francisella's virulence, location sensing and GSH stealing from host ScienceDirect Structural insights into glutathione mediated activation of the master regulator PrfA in Listeria monocytogenes Protein & Cell Springer Nature Link

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