Abstract
Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs. These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking α-helices from both subunits.
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Zhang, Rg., Joachimiak, A., Lawson, C. et al. The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity. Nature 327, 591–597 (1987). https://doi.org/10.1038/327591a0
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DOI: https://doi.org/10.1038/327591a0
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