THE X-RAY STRUCTURE OF THE GCN4-BZIP BOUND TO ATF CREB SITE DNA SHOWS THE COMPLEX DEPENDS ON DNA FLEXIBILITY
THE X-RAY STRUCTURE OF THE GCN4-BZIP BOUND TO ATF CREB SITE DNA SHOWS THE COMPLEX DEPENDS ON DNA FLEXIBILITY
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DOI：
10.1006/jmbi.1993.1490
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发表时间：
1993-09-05
影响因子：
5.6
通讯作者：
RICHMOND, TJ
中科院分区：
文献类型：
--
作者：
KONIG, P;RICHMOND, TJ
酵母转录激活蛋白GCN 4的DNA结合域与含有完全对称的ATF/CREB位点序列的DNA片段结合的X射线结构已被解析到3·0 μ m分辨率。这种特异性识别复合物的结构支持bZIP蛋白的当前模型：平行α-螺旋的同源二聚体形成螺旋间卷曲螺旋区亮氨酸拉链，并且两个N-末端碱性区域适合DNA双螺旋相对两侧的半位点的大沟。结构表明，DNA的灵活性在保持蛋白质与对称的ATF/CREB位点（ATGACGTCAT）相比，伪对称的AP-1靶位点（ATGACTCAT）的接触中起着主导作用，克服了ATF/CREB序列中心额外的G · C碱基对引入的功能基团的位置置换。
The X-ray structure of the DNA binding domain of the yeast transcriptional activator protein GCN4 bound to a DNA fragment containing the sequence of the perfectly symmetrical ATF/CREB site has been solved to 3·0 Å resolution. The architecture of this specific recognition complex supports the current model for bZIP proteins: a homodimer of parallel α-helices form an interhelix coiled-coil regionviathe leucine zipper, and the two N-terminal basic regions fit into the major groove of half sites on opposite sides of the DNA double helix. The structure shows that DNA flexibility plays the predominant role in the preservation of protein contacts with the symmetric ATF/CREB site (ATGACGTCAT) as compared to the psuedo-symmetric AP-1 target site (ATGACTCAT), overcoming the positional displacement of functional groups introduced by the additional G · C base-pair at the center of the ATF/CREB sequence.