3HTS
HEAT SHOCK TRANSCRIPTION FACTOR/DNA COMPLEX
Summary for 3HTS
Entry DOI | 10.2210/pdb3hts/pdb |
Descriptor | 5'-D(*GP*GP*TP*TP*CP*TP*AP*GP*AP*AP*CP*C)-3', HEAT SHOCK TRANSCRIPTION FACTOR, GLYCEROL, ... (4 entities in total) |
Functional Keywords | transcription regulation, dna-binding protein, complex (winged helix_turn_ helix-dna), transcription-dna complex, transcription/dna |
Biological source | Kluyveromyces lactis More |
Cellular location | Nucleus: P22121 |
Total number of polymer chains | 2 |
Total formula weight | 15695.91 |
Authors | Littlefield, O.,Nelson, H.C.M. (deposition date: 1998-11-16, release date: 1999-04-29, Last modification date: 2023-09-06) |
Primary citation | Littlefield, O.,Nelson, H.C. A new use for the 'wing' of the 'winged' helix-turn-helix motif in the HSF-DNA cocrystal. Nat.Struct.Biol., 6:464-470, 1999 Cited by PubMed Abstract: The 1.75 A crystal structure of the Kluyveromyces lactis heat shock transcription factor (HSF) DNA-binding domain (DBD) complexed with DNA reveals a protein-DNA interface with few direct major groove contacts and a number of phosphate backbone contacts that are primarily water-mediated interactions. The DBD, a 'winged' helix-turn-helix protein, displays a novel mode of binding in that the 'wing' does not contact DNA like all others of that class. Instead, the monomeric DBD, which crystallized as a symmetric dimer to a pair of nGAAn inverted repeats, uses the 'wing' to form part of the protein-protein contacts. This dimer interface is likely important for increasing the DNA-binding specificity and affinity of the trimeric form of HSF, as well as for increasing cooperativity between adjacent trimers. PubMed: 10331875DOI: 10.1038/8269 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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