5D5V

Crystal structure of human Hsf1 with Satellite III repeat DNA

Summary for 5D5V

• Entry DOI: 10.2210/pdb5d5v/pdb
• Descriptor: Heat shock factor protein 1, DNA, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: protein-dna complex, double helix, helix-turn-helix, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm: Q00613
• Total number of polymer chains: 4
• Total formula weight: 36474.66

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

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: 26727489
DOI: 10.1038/nsmb.3149

Experimental method

X-RAY DIFFRACTION (2.55 Å)