来自Pseudomonas syringae的MucD结构揭示了类似HtrA的血清蛋白酶的N端环介导的三元化
Ju Hyeong Kim1, Gwan Hee Lee1, Jae-Hee Jeong2
1College of Pharmacy, Chung-Ang University, Seoul, 06974, Republic of Korea; Department of Global Innovative Drugs, Graduate School of Chung-Ang University, Seoul, 06974, Republic of Korea.
Biochemical and biophysical research communications
|November 17, 2023
概括
这项研究揭示了Pseudomonas syringae MucD (psMucD) 的结构,这是一个HtrA血清蛋白质酶. 它阐明了psMucD的情况.
科学领域:
- 生物化学 生化学
- 结构生物学 结构生物学
- 微生物学 微生物学
背景情况:
- 蛋白质质量控制对细胞完整性至关重要,HtrA血清蛋白酶管理 prokaryotes 中的周等离子体折叠应激.
- 大肠杆菌有三个HtrA成员 (DegS,DegP,DegQ);MucD是一种涉及酸盐生物合成和应激反应的相关蛋白质.
- 假杆菌 (Pseudomonas syringae) 导致植物疾病和人类感染,需要了解其毒性因素,如MucD.
研究的目的:
- 为了确定来自Pseudomonas注射器 (psMucD) 的MucD的高分辨率结构.
- 描述psMucD的寡合状态及其三元化机制.
- 将psMucD的结构和功能与其他HtrA家族成员进行比较,并建模其催化过程.
主要方法:
- 高分辨率结构确定psMucD.
- 对psMucD寡合化的基于溶液的分析.
- 与同类HtrA蛋白酶的序列和结构比较.
- 对psMucD催化机制的建模.
主要成果:
- 结构显示psMucD是一种典型的HtrA血清蛋白酶,具有不同的蛋白酶和PDZ域.
- psMucD存在于溶液中的三元体,其N端环介导的三元化.
- 序列和结构分析突出显示了与其他HtrA蛋白酶相比保存和独特的特征.
结论:
- psMucD是一种结构特征的HtrA家族血清蛋白酶,来自Pseudomonas syringae.
- 它的三聚体结构由N端环介导,对其功能至关重要.
- 了解psMucD提供了对HtrA蛋白酶机制及其在细菌病原性中的作用的洞察.
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