2hts
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| , resolution 1.83Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE DNA BINDING DOMAIN OF THE HEAT SHOCK TRANSCRIPTION FACTOR
OverviewOverview
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.
About this StructureAbout this Structure
2HTS is a Single protein structure of sequence from Kluyveromyces lactis. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the DNA binding domain of the heat shock transcription factor., Harrison CJ, Bohm AA, Nelson HC, Science. 1994 Jan 14;263(5144):224-7. PMID:8284672
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