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大肠杆菌嘌呤阻遏物-次黄嘌呤-DNA复合物的结晶及初步X射线分析。

Crystallization and preliminary X-ray analysis of an Escherichia coli purine repressor-hypoxanthine-DNA complex.

作者信息

Schumacher M A, Choi K Y, Zalkin H, Brennan R G

机构信息

Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland 97201-3098.

出版信息

J Mol Biol. 1994 Sep 23;242(3):302-5. doi: 10.1006/jmbi.1994.1580.

Abstract

The purine repressor (PurR) is a DNA-binding protein, which together with a purine corepressor serves to regulate de novo purine and pyrimidine biosynthesis in Escherichia coli. PurR belongs to the structurally homologous lac repressor family of transcription regulators. A PurR-hypoxanthine-DNA complex has been crystallized, with DNA encompassing the high affinity purF operator site and which is 16 base-pairs long with 5'-deoxynucleoside overhangs on each complementary strand. The crystals diffract to better than 2.6 A and take the orthorhombic space group C222(1), with unit cell dimensions a = 175.9 A, b = 94.8 A and c = 81.8 A. The structure determination of this PurR-hypoxanthine-DNA complex will provide the first high resolution view of a Lacl member-DNA complex.

摘要

嘌呤阻遏蛋白(PurR)是一种DNA结合蛋白,它与嘌呤辅阻遏物共同作用,调节大肠杆菌中嘌呤和嘧啶的从头生物合成。PurR属于转录调节因子中结构同源的乳糖阻遏蛋白家族。PurR-次黄嘌呤-DNA复合物已结晶,DNA包含高亲和力的purF操纵位点,长16个碱基对,每条互补链上有5'-脱氧核苷突出端。这些晶体的衍射分辨率优于2.6 Å,属于正交空间群C222(1),晶胞尺寸为a = 175.9 Å,b = 94.8 Å,c = 81.8 Å。这种PurR-次黄嘌呤-DNA复合物的结构测定将提供Lacl成员-DNA复合物的首个高分辨率视图。

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