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Nature 327, 591 - 597 (18 June 1987); doi:10.1038/327591a0

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

Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois 60637, USA
*Permanent address: Shanghai Institute of Biochemistry, Chinese Academy of Sciences, Shanghai, People's Republic of China.
Present address: Institute of Bioorganic Chemistry, Polish Academy of Sciences, 61704 Poznan, Poland.
To whom correspondence should be addressed.

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.

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