Mondragón A, Harrison S C
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.
J Mol Biol. 1991 May 20;219(2):321-34. doi: 10.1016/0022-2836(91)90568-q.
The crystal structure of phage 434 Cro protein in complex with a 20 base-pair DNA fragment has been determined to 2.5 A resolution. The DNA fragment contains the sequence of the OR1 operator site. The structure shows a bent conformation for the DNA, straighter at the center and more bent at the ends. The central base-pairs adopt conformations with significant deviations from coplanarity. The two molecules interact extensively along their common interface, both through hydrogen bonds and van der Waals interactions. The significance of these interactions for operator binding and recognition is discussed.
已确定与一个20个碱基对的DNA片段形成复合物的噬菌体434 Cro蛋白的晶体结构,分辨率为2.5埃。该DNA片段包含OR1操纵基因位点的序列。结构显示DNA呈弯曲构象,中间较直,两端弯曲度更大。中央碱基对采取的构象与共平面性有显著偏差。两个分子沿着它们的共同界面广泛相互作用,通过氢键和范德华相互作用。讨论了这些相互作用对操纵基因结合和识别的意义。