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The three-dimensional structure of trp repressor

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Abstract

The crystal structure of the Escherichia coli trp repressor has been solved to atomic resolution. The dimeric protein has a remarkable subunit interface in which five of each subunit's six helices are interlinked. The binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix–turn–helix motif and by moulding the details of the repressor's structure near the DNA binding surface.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, The University of Chicago, 920 East 58th Street, Chicago, Illinois, 60637, USA

    Richard W. Schevitz, Zdzislaw Otwinowski, Andrzej Joachimiak, Catherine L. Lawson & Paul B. Sigler

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  1. Richard W. Schevitz
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  2. Zdzislaw Otwinowski
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  3. Andrzej Joachimiak
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  4. Catherine L. Lawson
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  5. Paul B. Sigler
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Schevitz, R., Otwinowski, Z., Joachimiak, A. et al. The three-dimensional structure of trp repressor. Nature 317, 782–786 (1985). https://doi.org/10.1038/317782a0

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