Recent applications of phage therapy in localized wound and drug-resistant bacterial infection have brought bacteriophage back to the spotlight. While these works demonstrated the safety and effectiveness of engineered bacteriophages in human patients, the exact molecular machinery behind the bacteria killing remains largely uncharacterized. This is particularly noticable outside Escherichia coli phages, as most studies are based on bacteriophages of this Gram-negative model bacterium. In the attempt to extent our understanding to the bacteriophage of Gram-positive bacteria, we chose the host hijacking module of Bacillus subtilis phage SPO1 for systemic functional and structural studies. Gp49, an acidic protein located within operon 4 of this module, is believed to have a role during the host takeover event. Here we describe the complete resonance assignment of Gp49, which shares no sequence homology with any known protein, as the basis for the structure determination and further mechanism study.

中文翻译：

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噬菌体SPO1 Gp49蛋白的共振分配。

噬菌体疗法在局部伤口和耐药细菌感染中的最新应用使噬菌体重新成为人们关注的焦点。尽管这些工作证明了工程化噬菌体在人类患者中的安全性和有效性，但杀死细菌背后的确切分子机制仍未明确。这在大肠杆菌噬菌体以外尤为明显，因为大多数研究都基于这种革兰氏阴性模型细菌的噬菌体。为了扩大我们对革兰氏阳性细菌噬菌体的了解，我们选择了枯草芽孢杆菌噬菌体SPO1的宿主劫持模块。用于系统功能和结构研究。Gp49是位于此模块操纵子4内的酸性蛋白，被认为在宿主接管事件中起作用。在这里，我们描述了Gp49的完全共振分配，它与任何已知的蛋白质均不具有序列同源性，作为结构确定和进一步机理研究的基础。