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Science 14 January 1994:
Vol. 263. no. 5144, pp. 224 - 227
DOI: 10.1126/science.8284672
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Articles

Science, Vol 263, Issue 5144, 224-227
Copyright © 1994 by American Association for the Advancement of Science

articles

Crystal structure of the DNA binding domain of the heat shock transcription factor

CJ Harrison, AA Bohm, and HC Nelson

Department of Molecular and Cell Biology, University of California, Berkeley 94720.

The structure of the DNA binding domain, determined at 1.8 angstrom resolution, contains a three-helix bundle that is capped by a four-stranded antiparallel beta sheet. This structure is a variant of the helix-turn-helix motif, typified by catabolite activator protein. In the heat shock transcription factor, the first helix of the motif (alpha 2) has an alpha-helical bulge and a proline-induced kink. The angle between the two helices of the motif (alpha 2 and alpha 3) is about 20 degrees smaller than the average for canonical helix-turn-helix proteins. Nevertheless, the relative positions of the first and third helices of the bundle (alpha 1 and alpha 3) are conserved. It is proposed here that the first helix of the three-helix bundle be considered a component of the helix-turn-helix motif.


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Crystal Structure of S-Adenosylmethionine Synthetase.
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