Silva M V, Pasternack L B, Kearns D R
Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla 92093, USA.
Arch Biochem Biophys. 1997 Dec 15;348(2):255-61. doi: 10.1006/abbi.1997.0377.
Transcription factor 1 (TF1), a type II DNA-binding protein encoded by the Bacillus subtilis bacteriophage SPO1, has the capacity for sequence-selective DNA binding and a preference for 5-hydroxymethyl-2'-deoxyuridine (HmU)-containing DNA. In NMR studies of the TF1/HmU-DNA complex, intermolecular NOEs indicate that the flexible beta-ribbon and C-terminal alpha-helix are involved in the DNA-binding site of TF1, placing it in the beta-sheet category of DNA-binding proteins proposed to bind by wrapping two beta-ribbon "arms" around the DNA. Intermolecular and intramolecular NOEs were used to generate an energy-minimized model of the protein-DNA complex in which both DNA bending and protein structure changes are evident.
转录因子1（TF1）是由枯草芽孢杆菌噬菌体SPO1编码的II型DNA结合蛋白，具有序列选择性DNA结合能力，且优先结合含5-羟甲基-2'-脱氧尿苷（HmU）的DNA。在TF1/HmU-DNA复合物的核磁共振研究中，分子间的核Overhauser效应（NOE）表明，柔性β- ribbon和C端α-螺旋参与了TF1的DNA结合位点，使其属于通过将两条β- ribbon“臂”缠绕在DNA周围而结合的DNA结合蛋白的β- sheet类别。分子间和分子内的NOE被用于生成蛋白质-DNA复合物的能量最小化模型，其中DNA弯曲和蛋白质结构变化都很明显。
