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    Expression, purification, crystallization and preliminary X-ray analysis of the DNA-binding domain of a Chlamydia trachomatis OmpR/PhoB-subfamily response regulator homolog, ChxR

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    Issue Date
    2009-08
    Author
    Hickey, John M.
    Hefty, P. Scott
    Lamb, Audrey L.
    Publisher
    International Union of Crystallography
    Type
    Article
    Article Version
    Scholarly/refereed, publisher version
    Metadata
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    Abstract
    Two-component signal transduction systems in bacteria are a primary mechan­ism for responding to environmental stimuli and adjusting gene expression accordingly. Generally in these systems a sensor kinase phosphorylates a response regulator that regulates transcription. Response regulators contain two domains: a receiver domain and an effector domain. The receiver domain is typically phosphorylated and as a result facilitates the DNA-binding and transcriptional activity of the effector domain. The OmpR/PhoB subfamily is the largest of the response-regulator subfamilies and is primarily defined by the winged helix-turn-helix DNA-binding motif within the effector domain. The overall structure of effector domains is highly conserved and contains three defined elements that are critical for transcriptional regulation: a DNA major-groove binding helix, a DNA minor-groove binding wing and a transcriptional activation loop. These functional elements are often diverse in sequence and conformation and reflect the functional differences observed between individual subfamily members. ChxR from Chlamydia trachomatis is an atypical OmpR/PhoB response regulator homolog that has transcriptional activity in the absence of phos­phorylation. To facilitate the precise identification of the functional elements of the ChxR effector domain, this protein was cloned, expressed, purified and crystallized. Crystals were obtained from two separate mother liquors, producing two morphologically distinct crystals. The space group of both crystals was P43212 (or its enantiomorph P41212) with isomorphous unit-cell parameters; the crystals diffracted to 2.2-2.5 Å resolution.
    Description
    This is the published version. Copyright 2009 by the International Union of Crystallography.
    URI
    http://hdl.handle.net/1808/17437
    DOI
    https://doi.org/10.1107/S1744309109025184
    Collections
    • Molecular Biosciences Scholarly Works [458]
    Citation
    Hickey, J. M., Scott Hefty, and Audrey L. Lamb. "Expression, Purification, Crystallization and Preliminary X-ray Analysis of the DNA-binding Domain of a Chlamydia Trachomatis OmpR/PhoB-subfamily Response Regulator Homolog, ChxR." Acta Crystallographica Section F Structural Biology and Crystallization Communications 65.8 (2009): 791-94. Wiley Online Library. Web. 17 Apr. 2015. http://dx.doi.org/10.1107/S1744309109025184.

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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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