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    Nature. 1985 Oct 31-Nov 6;317(6040):782-6.

    The three-dimensional structure of trp repressor.

    Schevitz RW, Otwinowski Z, Joachimiak A, Lawson CL, Sigler PB.

    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.

    PMID: 3903514 [PubMed - indexed for MEDLINE]

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