The crystal structure of the effector-binding domain of the trehalose repressor TreR from Bacillus subtilis 168 reveals a unique quarternary assembly

Authors

  • Pavlína Řezáčová,

    1. Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas
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  • Veronika Krejčiříková,

    1. Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas
    Current affiliation:
    1. Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
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  • Dominika Borek,

    1. Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas
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  • Shiu F. Moy,

    1. Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois
    2. Midwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory, Argonne, Illinois
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  • Andrzej Joachimiak,

    1. Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois
    2. Midwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory, Argonne, Illinois
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  • Zbyszek Otwinowski

    Corresponding author
    1. Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas
    • Department of Biochemistry, The University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-8816
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  • The manuscript has been created by UChicago Argonne, LLC, Operator of Argonne National Laboratory (“Argonne”). Argonne, a U.S. Department of Energy Office of Science laboratory, is operated under Contract No. DE-AC02-06CH11357. The U.S. Government retains for itself, and others acting on its behalf, a paid-up nonexclusive, irrevocable worldwide license in said article to reproduce, prepare derivative works, distribute copies to the public, and perform publicly and display publicly, by or on behalf of the Government.

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