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    Atypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA Binding

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    Issue Date
    2014-03-19
    Author
    Barta, Michael L.
    Hickey, John M.
    Anbanandam, Asokan
    Dyer, Kevin
    Hammel, Michal
    Hefty, P. Scott
    Publisher
    Public Library of Science
    Type
    Article
    Article Version
    Scholarly/refereed, publisher version
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    Abstract
    ChxR is an atypical two-component signal transduction response regulator (RR) of the OmpR/PhoB subfamily encoded by the obligate intracellular bacterial pathogen Chlamydia trachomatis. Despite structural homology within both receiver and effector domains to prototypical subfamily members, ChxR does not require phosphorylation for dimer formation, DNA binding or transcriptional activation. Thus, we hypothesized that ChxR is in a conformation optimal for DNA binding with limited interdomain interactions. To address this hypothesis, the NMR solution structure of the ChxR effector domain was determined and used in combination with the previously reported ChxR receiver domain structure to generate a full-length dimer model based upon SAXS analysis. Small-angle scattering of ChxR supported a dimer with minimal interdomain interactions and effector domains in a conformation that appears to require only subtle reorientation for optimal major/minor groove DNA interactions. SAXS modeling also supported that the effector domains were in a head-to-tail conformation, consistent with ChxR recognizing tandem DNA repeats. The effector domain structure was leveraged to identify key residues that were critical for maintaining protein - nucleic acid interactions. In combination with prior analysis of the essential location of specific nucleotides for ChxR recognition of DNA, a model of the full-length ChxR dimer bound to its cognate cis-acting element was generated.
    Description
    This is the published version. Copyright Public Library of Science
    URI
    http://hdl.handle.net/1808/19240
    DOI
    https://doi.org/10.1371/journal.pone.0091760
    Collections
    • Higuchi Biosciences Center Scholarly Works [51]
    Citation
    Barta, Michael L., John M. Hickey, Asokan Anbanandam, Kevin Dyer, Michal Hammel, and P. Scott Hefty. "Atypical Response Regulator ChxR from Chlamydia Trachomatis Is Structurally Poised for DNA Binding." PLoS ONE 9.3 (2014): n. pag. DOI:10.1371/journal.pone.0091760

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    KU Libraries
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    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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