Yersinia pestis, the causative agent of bubonic plague, is one of the most lethal pathogens in recorded human history. Today, the concern is the possible misuse of Y. pestis as an agent in bioweapons and bioterrorism. Current therapies for the treatment of plague include the use of a small number of antibiotics, but clinical cases of antibiotic resistance have been reported in some areas of the world. Therefore, the discovery of new drugs is required to combat potential Y. pestis infection. Here, the crystal structure of the Y. pestis UDP‐glucose pyrophosphorylase (UGP), a metabolic enzyme implicated in the survival of Y. pestis in mouse macrophages, is described at 2.17 Å resolution. The structure provides a foundation that may enable the rational design of inhibitors and open new avenues for the development of antiplague therapeutics.

中文翻译：

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来自鼠疫耶尔森菌的 UDP-葡萄糖焦磷酸化酶的晶体结构，鼠疫的潜在治疗靶点。


鼠疫耶尔森氏菌是黑死病的病原体，是人类历史上最致命的病原体之一。如今，令人担忧的是鼠疫杆菌可能被滥用作为生物武器和生物恐怖主义的媒介。目前治疗鼠疫的疗法包括使用少量抗生素，但世界某些地区已报告了抗生素耐药性的临床病例。因此，需要发现新药来对抗潜在的鼠疫耶尔森氏菌感染。在此，以 2.17 Å 分辨率描述了鼠疫耶尔森氏菌UDP-葡萄糖焦磷酸化酶 (UGP) 的晶体结构，UGP 是一种与鼠疫耶尔森氏菌在小鼠巨噬细胞中存活有关的代谢酶。该结构为合理设计抑制剂奠定了基础，并为抗鼠疫疗法的开发开辟了新途径。