CO-CRYSTAL STRUCTURE OF TBP RECOGNIZING THE MINOR-GROOVE OF A TATA ELEMENT
CO-CRYSTAL STRUCTURE OF TBP RECOGNIZING THE MINOR-GROOVE OF A TATA ELEMENT
复制标题
DOI：
10.1038/365520a0
复制
发表时间：
1993-10-07
期刊：
影响因子：
64.8
通讯作者：
BURLEY, SK
中科院分区：
文献类型：
--
作者：
KIM, JL;NIKOLOV, DB;BURLEY, SK
与腺病毒主要晚期启动子的TATA元件复合的TATA盒结合多肽的三维结构已通过X射线晶体学在2.25埃分辨率下测定。鞍形蛋白的结合诱导DNA的构象变化，在序列TATAAAAG的任一末端诱导尖锐的扭结。在扭结之间，右手双螺旋平滑弯曲并部分解绕，对TBP的凹形反平行β折叠呈现出加宽的小沟。侧链/碱基相互作用仅限于小沟，包括氢键、货车范德华接触和苯丙氨酸-碱基堆积相互作用。
The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter ha's been determined by X-ray crystallography at 2.25 angstrom resolution. Binding of the saddle-shaped protein induces a conformational change in the DNA, inducing sharp kinks at either end of the sequence TATAAAAG. Between the kinks, the right-handed double helix is smoothly curved and partially unwound, presenting a widened minor groove to TBP's concave, antiparallel beta-sheet. Side-chain/base interactions are restricted to the minor groove, and include hydrogen bonds, van der Waals contacts and phenylalanine-base stacking interactions.