1FYM
SERENDIPITOUS CRYSTAL STRUCTURE CONTAINING THE HEAT SHOCK TRANSCRIPTION FACTOR'S DNA BINDING DOMAIN AND COGNATE DNA IN A TAIL-TO-TAIL ORIENTATION
1FYM の概要
| エントリーDOI | 10.2210/pdb1fym/pdb |
| 関連するPDBエントリー | 1FYK 1FYL 2HTS 3HTS |
| 分子名称 | TAIL-TO-TAIL HSE, HEAT SHOCK TRANSCRIPTION PROTEIN (3 entities in total) |
| 機能のキーワード | crystal-packing interface, crystallization, protein-dna interface, protein-protein interface, static disorder, transcription-dna complex, transcription/dna |
| 由来する生物種 | Kluyveromyces lactis 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 29225.37 |
| 構造登録者 | |
| 主引用文献 | Littlefield, O.,Nelson, H.C. Crystal packing interaction that blocks crystallization of a site-specific DNA binding protein-DNA complex. Proteins, 45:219-228, 2001 Cited by PubMed Abstract: We present here three high-resolution crystal structures of complexes between the DNA-binding domain of the heat-shock transcription factor (HSF) and DNA oligomers. Although the DNA oligomers contain HSF's specific binding sequence, called a heat-shock element, the crystal structures do not contain the specific protein-DNA complex. In one crystal structure, the 10 base pair DNA oligomer is statically disordered. In the other two related structures, the 12 base pair DNA oligomers are in unique positions, but the protein-DNA contacts in these two crystals are not sequence specific. In all three structures, the DNA appears to act as a rigid, polyanion scaffold to support columns of proteins in a crystalline lattice. A robust crystal packing interface between protein monomers obscures the true DNA-binding surface, known from previous genetic and biochemical studies. By redesigning the protein to interfere with the crystal lattice contacts, we were able to obtain physiologically relevant crystals in a specific protein-DNA complex. Thus, a crystal-packing interface was able to prevent the weak, but physiological relevant interactions between a protein and DNA. PubMed: 11599025DOI: 10.1002/prot.1142 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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