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Science 11 November 1988:
Vol. 242. no. 4880, pp. 893 - 899
DOI: 10.1126/science.3187530
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Articles

Science, Vol 242, Issue 4880, 893-899
Copyright © 1988 by American Association for the Advancement of Science

articles

Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions

Jordan SR and CO Pabo

Department of Biophysics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205.

The crystal structure of a complex containing the DNA-binding domain of lambda repressor and a lambda operator site was determined at 2.5 A resolution and refined to a crystallographic R factor of 24.2 percent. The complex is stabilized by an extensive network of hydrogen bonds between the protein and the sugar-phosphate backbone. Several side chains form hydrogen bonds with sites in the major groove, and hydrophobic contacts also contribute to the specificity of binding. The overall arrangement of the complex is quite similar to that predicted from earlier modeling studies, which fit the protein dimer against linear B-form DNA. However, the cocrystal structure reveals important side chain-side chain interactions that were not predicted from the modeling or from previous genetic and biochemical studies.


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