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Nature. 1987 Jun 18-24;327(6123):591-7.

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


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 alpha-helices from both subunits.

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