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- W2077117400 abstract "The Xanthomonas campestris transcription regulator OhrR contains a reactive cysteine residue (C22) that upon oxidation by organic hydroperoxides (OHPs) forms an intersubunit disulphide bond with residue C127'. Such modification induces the expression of a peroxidase that reduces OHPs to their less toxic alcohols. Here, we describe the structures of reduced and OHP-oxidized OhrR, visualizing the structural mechanism of OHP induction. Reduced OhrR takes a canonical MarR family fold with C22 and C127' separated by 15.5 A. OHP oxidation results in the disruption of the Y36'-C22-Y47' interaction network and dissection of helix alpha5, which then allows the 135 degrees rotation and 8.2 A translation of C127', formation of the C22-C127' disulphide bond, and alpha6-alpha6' helix-swapped reconfiguration of the dimer interface. These changes result in the 28 degrees rigid body rotations of each winged helix-turn-helix motif and DNA dissociation. Similar effector-induced rigid body rotations are expected for most MarR family members." @default.
- W2077117400 created "2016-06-24" @default.
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- W2077117400 date "2007-11-01" @default.
- W2077117400 modified "2023-10-17" @default.
- W2077117400 title "Structural Mechanism of Organic Hydroperoxide Induction of the Transcription Regulator OhrR" @default.
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- W2077117400 doi "https://doi.org/10.1016/j.molcel.2007.09.016" @default.
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