Publication: Structural Mechanism of Organic Hydroperoxide Induction of the Transcription Regulator OhrR
Issued Date
2007-11-30
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ISSN
10972765
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2-s2.0-36248933266
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Mahidol University
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SCOPUS
Bibliographic Citation
Molecular Cell. Vol.28, No.4 (2007), 652-664
Suggested Citation
Kate J. Newberry, Mayuree Fuangthong, Warunya Panmanee, Skorn Mongkolsuk, Richard G. Brennan Structural Mechanism of Organic Hydroperoxide Induction of the Transcription Regulator OhrR. Molecular Cell. Vol.28, No.4 (2007), 652-664. doi:10.1016/j.molcel.2007.09.016 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/24080
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Title
Structural Mechanism of Organic Hydroperoxide Induction of the Transcription Regulator OhrR
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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 Å. OHP oxidation results in the disruption of the Y36′-C22-Y47′ interaction network and dissection of helix α5, which then allows the 135° rotation and 8.2 Å translation of C127′, formation of the C22-C127′ disulphide bond, and α6-α6′ helix-swapped reconfiguration of the dimer interface. These changes result in the 28° 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. © 2007 Elsevier Inc. All rights reserved.