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Article
Nature 335, 321 - 329 (22 September 1988); doi:10.1038/335321a0

Crystal structure of trp represser/operator complex at atomic resolution

Z. Otwinowski, R. W. Schevitz*, R.-G. Zhang, C. L. Lawson*, A. Joachimiak*, R. Q. Marmorstein, B. F. Luisi & P. B. Sigler§

Department of Biochemistry and Molecular Biology, and Department of Chemistry, University of Chicago, 920 East 58 Street, Chicago, Illinois 60637, USA
*Present addresses: Lilly Research Laboratories, Indianapolis, Indiana 46285, USA (R.W.S.); Department of Physical Chemistry, N. Rijksuniversitat, Groningen, The Netherlands (C.L.L.); Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland (A.J.).
Permanent address: Chinese Academy of Sciences, Institute of Biochemistry, Shanghai, Republic of China.
§To whom correspondence should be addressed.

The crystal structure of the trp repressor/operator complex shows an extensive contact surface, including 24 direct and 6 solvent-mediated hydrogen bonds to the phosphate groups of the DNA. There are no direct hydrogen bonds or non-polar contacts to the bases that can explain the repressor's specificity for the operator sequence. Rather, the sequence seems to be recognized indirectly through its effects on the geometry of the phosphate backbone, which in turn permits the formation of a stable interface. Water-mediated polar contacts to the bases also appear to contribute part of the specificity.

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