CRYSTAL-STRUCTURE OF YEAST TATA-BINDING PROTEIN AND MODEL FOR INTERACTION WITH DNA
CRYSTAL-STRUCTURE OF YEAST TATA-BINDING PROTEIN AND MODEL FOR INTERACTION WITH DNA
复制标题
DOI：
10.1073/pnas.90.17.8174
复制
发表时间：
1993-09-01
影响因子：
11.1
通讯作者：
KORNBERG, RD
中科院分区：
文献类型：
--
作者：
CHASMAN, DI;FLAHERTY, KM;KORNBERG, RD
酵母(Saccharmyces Cerevisiae)TATA结合蛋白(TBP)的C端179-AA区在系统发育上是保守的，具有足够的功能，形成的晶体分辨率可达1.7埃。该蛋白质的结构由拟南芥TBP坐标的分子置换确定，并细化到2.6埃，在两个结构几乎相同的亚域之间略有不同，夹角约为12度，表明了一定程度的构象灵活性。提出了TBP-DNA相互作用的模型，具有以下重要特征：蛋白质的长尺寸遵循小槽的轨迹；亚域之间保守的两排碱性残基沿着蛋白质的边缘靠近DNA磷酸盐；一条疏水残基沿着槽的中央延伸；突变导致TATA序列第二个碱基特异性改变的氨基酸残基并列在该碱基上。
The C-terminal 179-aa region of yeast (Saccharomyces cerevisiae) TATA-binding protein (TBP), phylogenetically conserved and sufficient for many functions, formed crystals diffracting to 1.7-angstrom resolution. The structure of the protein, determined by molecular replacement with coordinates from Arabidopsis TBP and refined to 2.6 angstrom, differed from that in Arabidopsis slightly by an angle of about 12-degrees between two structurally nearly identical subdomains, indicative of a degree of conformational flexibility. A model for TBP-DNA interaction is proposed with the following important features: the long dimension of the protein follows the trajectory of the minor groove; two rows of basic residues conserved between the subdomains lie along the edges of the protein in proximity to the DNA phosphates; a band of hydrophobic residues runs down the middle of the groove; and amino acid residues whore mutation alters specificity for the second base of the TATA sequence are juxtaposed to that base.