Crystal Structure of the DNA Binding Domain of the Heat Shock Transcription Factor
- 14 January 1994
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 263 (5144) , 224-227
- https://doi.org/10.1126/science.8284672
Abstract
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.Keywords
This publication has 47 references indexed in Scilit:
- Helix geometry in proteinsPublished by Elsevier ,2004
- Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linkingProtein Engineering, Design and Selection, 1994
- TRANSCRIPTION FACTORS: Structural Families and Principles of DNA RecognitionAnnual Review of Biochemistry, 1992
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Trimerization of a yeast transcriptional activator via a coiled-coil motifCell, 1989
- Domains of the SFL1 protein of yeasts are homologous to Myc oncoproteins or yeast heat-shock transcription factorGene, 1989
- Isolation of the gene encoding the S. cerevisiae heat shock transcription factorCell, 1988
- The MIDAS display systemJournal of Molecular Graphics, 1988
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- Structural invariants in protein foldingNature, 1975