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识别TATAAAAG小沟的TBP的分辨率提高的结构

1.9 A resolution refined structure of TBP recognizing the minor groove of TATAAAAG.

作者信息

Kim J L, Burley S K

机构信息

Laboratory of Molecular Biophysics, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021, USA.

出版信息

Nat Struct Biol. 1994 Sep;1(9):638-53. doi: 10.1038/nsb0994-638.

Abstract

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 A 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.

摘要

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拟南芥TATA盒结合蛋白(TBP)的三维结构已在1.9埃分辨率下得到优化,最终晶体学R因子为19.4%。单体马鞍形α/β蛋白的结合在DNA中诱导了前所未有的构象变化。本文对这种异常的蛋白质-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元件识别和起始前复合物组装的机制。

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