来自表皮葡萄球菌噬菌体CNPH82的重组门蛋白是一个13个亚基的低聚物。

Weisha Luan, Jochen Fesseler, Maria Chechik, Carina R Buttner, Alfred A Antson, Callum Smits
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引用次数: 3

摘要

噬菌体CNPH82的门蛋白cn3被预测为病毒基因组易位到预先形成的前衣壳中的途径,就像来自其他双链DNA尾噬菌体的门蛋白一样。噬菌体CNPH82的宿主是机会性人类致病细菌表皮葡萄球菌,是医院感染的主要原因。该噬菌体的门蛋白已被克隆、过表达和纯化。尺寸排阻色谱多角度激光散射分析表明,门脉蛋白含有~13个亚基。门脉蛋白晶体,衍射至4.2 Å。这些晶体属于空间群C222(1),晶胞参数为a=252.4,b=367.0,c=175.5 Å。自转函数显示在不对称单元中存在单个13亚基低聚物。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Recombinant portal protein from Staphylococcus epidermidis bacteriophage CNPH82 is a 13-subunit oligomer.

The portal protein cn3 of bacteriophage CNPH82 is predicted to serve as a gateway for translocation of viral genome into preformed pro-capsid, like portal proteins from other double-stranded DNA tailed bacteriophages. The host of bacteriophage CNPH82 is the opportunistic human pathogenic bacterium Staphylococcus epidermidis, a major cause of nosocomial infections. The portal protein of this phage has been cloned, overexpressed and purified. Size-exclusion chromatography-multi-angle laser light scattering analysis has indicated that the portal protein contains ∼13 subunits. Crystals of the portal protein, diffracting to 4.2 Å, have been obtained. These crystals belong to the space group C222(1) with the unit-cell parameters of a = 252.4, b = 367.0, c = 175.5 Å. The self-rotation function revealed the presence of a single 13-subunit oligomer in the asymmetric unit.

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期刊介绍: Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.
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