Structural highlights
Function
[HSF_KLULA] DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. Also required for growth at normal temperatures.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Harrison CJ, Bohm AA, Nelson HC. Crystal structure of the DNA binding domain of the heat shock transcription factor. Science. 1994 Jan 14;263(5144):224-7. PMID:8284672
