The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity

R. G. Zhang, A. Joachimiak, C. L. Lawson, R. W. Schevitz, Z. Otwinowski, P. B. Sigler

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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.

Original languageEnglish (US)
Pages (from-to)591-597
Number of pages7
JournalNature
Volume327
Issue number6123
DOIs
StatePublished - Jan 1 1987

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Zhang, R. G., Joachimiak, A., Lawson, C. L., Schevitz, R. W., Otwinowski, Z., & Sigler, P. B. (1987). The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity. Nature, 327(6123), 591-597. https://doi.org/10.1038/327591a0