1.9-ANGSTROM RESOLUTION REFINED STRUCTURE OF TBP RECOGNIZING THE MINOR-GROOVE OF TATAAAAG
1.9-ANGSTROM RESOLUTION REFINED STRUCTURE OF TBP RECOGNIZING THE MINOR-GROOVE OF TATAAAAG
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DOI：
10.1038/nsb0994-638
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发表时间：
1994-09-01
期刊：
影响因子：
--
通讯作者：
BURLEY, SK
中科院分区：
文献类型：
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作者：
KIM, JL;BURLEY, SK
来自拟南芥的 TATA 盒结合蛋白 (TBP) 与带有腺病毒主要晚期启动子 TATA 元件的 14 个碱基对寡核苷酸复合的三维结构已在 1.9 埃分辨率下进行了细化，最终晶体学 R 因子为 19.4%。单体、鞍形 α/β 蛋白的结合引起 DNA 中前所未有的构象变化。对这种不寻常的蛋白质-DNA 复合物进行了详细的结构和功能分析，特别强调了 DNA 变形、TATA 元件识别和预启动复合物组装的机制。
The three-dimensional structure of a TATA box-binding protein (TBP) from Arabidopsis thaliana complexed with a fourteen base pair oligonucleotide bearing the Adenovirus major late promoter TATA element has been refined at 1.9 Angstrom resolution, giving a final crystallographic R-factor of 19.4%. Binding of the monomeric, saddle-shaped alpha/beta protein induces an unprecedented conformational change in the DNA. A detailed structural and functional analysis of this unusual protein-DNA complex is presented, with particular emphasis on the mechanisms of DNA deformation, TATA element recognition, and preinitiation complex assembly.