THE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA-HELICES - CRYSTAL-STRUCTURE OF THE PROTEIN-DNA COMPLEX
THE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA-HELICES - CRYSTAL-STRUCTURE OF THE PROTEIN-DNA COMPLEX
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DOI：
10.1016/s0092-8674(05)80070-4
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发表时间：
1992-12-24
期刊：
影响因子：
64.5
通讯作者：
HARRISON, SC
中科院分区：
文献类型：
--
作者：
ELLENBERGER, TE;BRANDL, CJ;HARRISON, SC
酵母转录激活因子GCN4是已鉴定的30多种含有碱性区域亮氨酸拉链（bZIP）DNA结合基序的真核蛋白质中的一种。我们已经测定了GCN4 bZIP元件与DNA形成的复合物在2.9埃分辨率下的晶体结构。bZIP二聚体是一对连续的α螺旋，在其羧基末端30个残基上形成平行的卷曲螺旋，并逐渐朝其氨基末端发散，穿过DNA结合位点的大沟。卷曲螺旋二聚化界面几乎与DNA轴垂直，使复合物呈现字母T的形状。bZIP单体中没有扭结或急剧弯曲。bZIP蛋白质家族中保守的碱性区域残基与DNA碱基和磷酸氧原子有大量接触。bZIP二聚体与DNA相互作用的细节可以解释GCN4蛋白对AP - 1位点的识别。
The yeast transcriptional activator GCN4 is 1 of over 30 identified eukaryotic proteins containing the basic region leucine zipper (bZIP) DNA-binding motif. We have determined the crystal structure of the GCN4 bZIP element complexed with DNA at 2.9 angstrom resolution. The bZIP dimer is a pair of continuous alpha helices that form a parallel coiled coil over their carboxy-terminal 30 residues and gradually diverge toward their amino termini to pass through the major groove of the DNA-binding site. The coiled-coil dimerization interface is oriented almost perpendicular to the DNA axis, giving the complex the appearance of the letter T. There are no kinks or sharp bends in either bZIP monomer. Numerous contacts to DNA bases and phosphate oxygens are made by basic region residues that are conserved in the bZIP protein family. The details of the bZIP dimer interaction with DNA can explain recognition of the AP-1 site by the GCN4 protein.