A new use for the 'wing' of the 'winged' helix-turn-helix motif in the HSF–DNA cocrystal

摘要: 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 few direct major groove contacts and number phosphate backbone that are primarily water-mediated interactions. DBD, 'winged' helix-turn-helix protein, displays novel mode binding in 'wing' does not contact like all others class. Instead, monomeric which crystallized as symmetric dimer to pair nGAAn inverted repeats, uses form part protein-protein contacts. This is likely important for increasing specificity affinity trimeric HSF, well cooperativity between adjacent trimers.