5D5W
Crystal structure of Chaetomium thermophilum Skn7 with HSE DNA
Summary for 5D5W
| Entry DOI | 10.2210/pdb5d5w/pdb |
| Descriptor | HSE DNA, Putative transcription factor (3 entities in total) |
| Functional Keywords | protein-dna complex, double helix, helix-turn-helix, transcription |
| Biological source | Chaetomium thermophilum More |
| Total number of polymer chains | 2 |
| Total formula weight | 16280.44 |
| Authors | Neudegger, T.,Verghese, J.,Hayer-Hartl, M.,Hartl, F.U.,Bracher, A. (deposition date: 2015-08-11, release date: 2015-12-30, Last modification date: 2024-01-10) |
| Primary citation | Neudegger, T.,Verghese, J.,Hayer-Hartl, M.,Hartl, F.U.,Bracher, A. Structure of human heat-shock transcription factor 1 in complex with DNA. Nat.Struct.Mol.Biol., 23:140-146, 2016 Cited by PubMed Abstract: Heat-shock transcription factor 1 (HSF1) has a central role in mediating the protective response to protein conformational stresses in eukaryotes. HSF1 consists of an N-terminal DNA-binding domain (DBD), a coiled-coil oligomerization domain, a regulatory domain and a transactivation domain. Upon stress, HSF1 trimerizes via its coiled-coil domain and binds to the promoters of heat shock protein-encoding genes. Here, we present cocrystal structures of the human HSF1 DBD in complex with cognate DNA. A comparative analysis of the HSF1 paralog Skn7 from Chaetomium thermophilum showed that single amino acid changes in the DBD can switch DNA binding specificity, thus revealing the structural basis for the interaction of HSF1 with cognate DNA. We used a crystal structure of the coiled-coil domain of C. thermophilum Skn7 to develop a model of the active human HSF1 trimer in which HSF1 embraces the heat-shock-element DNA. PubMed: 26727489DOI: 10.1038/nsmb.3149 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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