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

The three-dimensional structure of trp repressor.

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.

PMID:
3903514
[PubMed - indexed for MEDLINE]
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