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Science 4 November 1994:
Vol. 266. no. 5186, pp. 763 - 770
DOI: 10.1126/science.7973627
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Articles

Science, Vol 266, Issue 5186, 763-770
Copyright © 1994 by American Association for the Advancement of Science

articles

Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices

MA Schumacher, KY Choi, H Zalkin, and RG Brennan

Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland 97201-3098.

The three-dimensional structure of a ternary complex of the purine repressor, PurR, bound to both its corepressor, hypoxanthine, and the 16-base pair purF operator site has been solved at 2.7 A resolution by x-ray crystallography. The bipartite structure of PurR consists of an amino-terminal DNA-binding domain and a larger carboxyl-terminal corepressor binding and dimerization domain that is similar to that of the bacterial periplasmic binding proteins. The DNA-binding domain contains a helix-turn-helix motif that makes base-specific contacts in the major groove of the DNA. Base contacts are also made by residues of symmetry-related alpha helices, the "hinge" helices, which bind deeply in the minor groove. Critical to hinge helix-minor groove binding is the intercalation of the side chains of Leu54 and its symmetry-related mate, Leu54', into the central CpG-base pair step. These residues thereby act as "leucine levers" to pry open the minor groove and kink the purF operator by 45 degrees.


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