2HTS
CRYSTAL STRUCTURE OF THE DNA BINDING DOMAIN OF THE HEAT SHOCK TRANSCRIPTION FACTOR
Summary for 2HTS
Entry DOI | 10.2210/pdb2hts/pdb |
Descriptor | HEAT-SHOCK TRANSCRIPTION FACTOR, ACETIC ACID (3 entities in total) |
Functional Keywords | transcription factor |
Biological source | Kluyveromyces lactis |
Cellular location | Nucleus: P22121 |
Total number of polymer chains | 1 |
Total formula weight | 11070.38 |
Authors | Harrison, C.,Nelson, H. (deposition date: 1994-06-02, release date: 1995-02-07, Last modification date: 2024-02-14) |
Primary citation | Harrison, C.J.,Bohm, A.A.,Nelson, H.C. Crystal structure of the DNA binding domain of the heat shock transcription factor. Science, 263:224-227, 1994 Cited by PubMed 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. PubMed: 8284672PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
Download full validation report
