TFIID TATA 框结合蛋白的晶体结构

Crystal structure of TFIID TATA-box binding protein.

作者信息

Nikolov D B, Hu S H, Lin J, Gasch A, Hoffmann A, Horikoshi M, Chua N H, Roeder R G, Burley S K

机构信息

Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021-6399.

出版信息

Nature. 1992 Nov 5;360(6399):40-6. doi: 10.1038/360040a0.

DOI:10.1038/360040a0

PMID:1436073

Abstract

The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIID tau) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 A resolution. This highly symmetric alpha/beta structure contains a new DNA-binding fold, resembling a molecular 'saddle' that sits astride the DNA. The DNA-binding surface is a curved, antiparallel beta-sheet. When bound to DNA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins.

摘要

已通过X射线晶体学在2.6埃分辨率下确定了真核转录装置核心组件之一——来自拟南芥的TATA框结合蛋白（TBP或TFIID tau）的结构。这种高度对称的α/β结构包含一种新的DNA结合折叠，类似于跨坐在DNA上的分子“鞍座”。DNA结合表面是一个弯曲的反平行β折叠片。当与DNA结合时，鞍座的凸面将呈现出来以便与其他转录起始因子和调节蛋白相互作用。