The three-dimensional structure of trp repressor

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

Research output: Contribution to journalArticle

264 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)782-786
Number of pages5
Issue number6040
StatePublished - Dec 1 1985

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    Schevitz, R. W., Otwinowski, Z., Joachimiak, A., Lawson, C. L., & Sigler, P. B. (1985). The three-dimensional structure of trp repressor. Nature, 317(6040), 782-786.