PF1 VIRUS STRUCTURE - HELICAL COAT PROTEIN AND DNA WITH PARAXIAL PHOSPHATES
PF1 VIRUS STRUCTURE - HELICAL COAT PROTEIN AND DNA WITH PARAXIAL PHOSPHATES
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DOI：
10.1126/science.8036516
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发表时间：
1994-07-29
期刊：
影响因子：
56.9
通讯作者：
DAY, LA
中科院分区：
文献类型：
--
作者：
LIU, DJ;DAY, LA
丝状噬菌体Pf 1中DNA的螺旋路径是从不同种类的现有结构信息推导出来的，包括来自X射线纤维衍射的结果。DNA的螺距与周围蛋白质亚单位的螺旋相同，为16埃;每个核苷酸的上升和旋转分别为6.1埃和132度;磷酸盐距离轴为2.5埃。因此，Pf 1中的DNA是已知的最延伸和扭曲的DNA结构。基于DNA结构和蛋白质的大量额外信息，提出了一个病毒体模型。在该模型中，DNA碱基延伸到蛋白质中，赖氨酸和精氨酸侧链延伸到DNA碱基之间，以稳定近轴磷酸电荷;蛋白质亚基的构象是α和3（10）螺旋的组合。
The helical path of the DNA in filamentous bacteriophage Pf1 was deduced from different kinds of existing structural information, including results from x-ray fiber diffraction. The DNA has the same pitch, 16 angstroms, as the surrounding helix of protein subunits; the rise and rotation per nucleotide are 6.1 angstroms and 132 degrees, respectively; and the phosphates are 2.5 angstroms from the axis. The DNA in Pf1 is, therefore, the most extended and twisted DNA structure known. On the basis of the DNA structure and extensive additional information about the protein, a model of the virion is proposed. In the model, the DNA bases reach out, into the protein, and the lysine and arginine side chains reach in, between the DNA bases, to stabilize the paraxial phosphate charges; the conformation of the protein subunit is combination of alpha and 3(10) helices.