MECHANISM OF COREPRESSOR-MEDIATED SPECIFIC DNA-BINDING BY THE PURINE REPRESSOR
MECHANISM OF COREPRESSOR-MEDIATED SPECIFIC DNA-BINDING BY THE PURINE REPRESSOR
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DOI：
10.1016/0092-8674(95)90243-0
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发表时间：
1995-10-06
期刊：
影响因子：
64.5
通讯作者：
BRENNAN, RG
中科院分区：
文献类型：
--
作者：
SCHUMACHER, MA;CHOI, KY;BRENNAN, RG
通过小分子效应物对同源DNA位点的DNA结合蛋白的亲和力的调节对于原核生物和真核生物都是常见的。然而，效应子与一个结构域的结合影响远端结构域的DNA结合的机制在结构上知之甚少。在最初的研究中，提供深入了解的乳糖阻遏家族的效应调节的DNA结合的机制，我们确定了嘌呤阻遏物的晶体结构结合到辅阻遏物和purF运营商。为了扩展我们的理解，我们已经确定了在2.2埃分辨率的嘌呤阻遏物的辅阻遏物自由辅阻遏物结合结构域的结构。在未配体状态下，辅阻遏物结合口袋中的结构变化导致每个亚基旋转打开多达23度，其结果是小沟结合铰链螺旋的脱离和阻遏物-DNA解离。
The modulation of the affinity of DNA-binding proteins by small molecule effecters for cognate DNA sites is common to both prokaryotes and eukaryotes. However, the mechanisms by which effector binding to one domain affects DNA binding by a distal domain are poorly understood structurally. In initial studies to provide insight into the mechanism of effector-modulated DNA binding of the lactose repressor family, we determined the crystal structure of the purine repressor bound to a corepressor and purF operator. To extend our understanding, we have determined the structure of the corepressor-free corepressor-binding domain of the purine repressor at 2.2 Angstrom resolution. In the unliganded state, structural changes in the corepressor-binding pocket cause each subunit to rotate open by as much as 23 degrees, the consequences of which are the disengagement of the minor groove-binding hinge helices and repressor-DNA dissociation.