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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >12-Fold symmetry of the putative portal protein from the Thermus thermophilus bacteriophage G20C determined by X-ray analysis
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12-Fold symmetry of the putative portal protein from the Thermus thermophilus bacteriophage G20C determined by X-ray analysis

机译：通过X射线分析确定嗜热栖热菌G20C的推定门户蛋白的12倍对称性

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摘要

In tailed bacteriophages and several animal viruses, the portal protein forms the gateway through which viral DNA is translocated into the head structure during viral particle assembly. In the mature virion the portal protein exists as a dodecamer, while recombinant portal proteins from several phages, including SPP1 and CNPH82, have been shown to form 13-subunit assemblies. A putative portal protein from the thermostable bacteriophage G20C has been cloned, overexpressed and purified. Crystals of the protein diffracted to 2.1 angstrom resolution and belonged to space group P42(1)2, with unit-cell parameters a = b = 155.3, c = 115.4 angstrom. The unit-cell content and self-rotation function calculations indicate that the protein forms a circular 12-subunit assembly.
机译：在尾巴噬菌体和几种动物病毒中，门禁蛋白形成了门户，病毒颗粒组装过程中病毒DNA通过该门户转移到头部结构中。在成熟病毒体中，门蛋白以十二聚体形式存在，而来自几种噬菌体（包括SPP1和CNPH82）的重组门蛋白已显示形成13个亚基组装体。来自热稳定噬菌体G20C的推定门户蛋白已被克隆，过表达和纯化。蛋白质晶体衍射至2.1埃分辨率，属于空间群P42（1）2，单位细胞参数a = b = 155.3，c = 115.4埃。单位细胞含量和自转功能的计算表明该蛋白质形成了一个环状的12个亚基组装体。

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