6MNU

Crystal structure of Yersinia pestis UDP-glucose pyrophosphorylase

6MNU の概要

• エントリーDOI: 10.2210/pdb6mnu/pdb
• 分子名称: UTP--glucose-1-phosphate uridylyltransferase, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: udp-glucose pyrophosphorylase, plague, yersinia pestis, transferase
• 由来する生物種: Yersinia pestis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 129358.62

構造登録者

Gibbs, M.E.,Lountos, G.T.,Gumpena, R.,Waugh, D.S. (登録日: 2018-10-03, 公開日: 2019-09-11, 最終更新日: 2023-10-11)

主引用文献

Gibbs, M.E.,Lountos, G.T.,Gumpena, R.,Waugh, D.S.
Crystal structure of UDP-glucose pyrophosphorylase from Yersinia pestis, a potential therapeutic target against plague.
Acta Crystallogr.,Sect.F, 75:608-615, 2019

PubMed Abstract: 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.

PubMed: 31475928
DOI: 10.1107/S2053230X19011154

実験手法

X-RAY DIFFRACTION (2.172 Å)