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雷利亚burgdorferi依赖ATP的金属蛋白酶FtsH在其功能相关的六合体形式的结构
Kalvis Brangulis1, Laura Drunka2, Inara Akopjana2
1Latvian Biomedical Research and Study Centre, Ratsupites 1 k-1, LV-1067 Riga, Latvia; Department of Human Physiology and Biochemistry, Riga Stradins University, Dzirciema 16, LV-1007 Riga, Latvia.
Biochimica et biophysica acta. Proteins and proteomics
|October 18, 2023
概括
波雷莉亚burgdorferi的BB0789蛋白质的晶体结构揭示了它的六米环结构,对于其蛋白酶和ATPase活动至关重要. 这种蛋白质对于莱姆病的生存和传播至关重要.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 微生物学 微生物学
背景情况:
- 依赖ATP的蛋白酶FtsH对于各种生物体中的蛋白质降解至关重要.
- FtsH同源BB0789对Borrelia burgdorferi的感染性和生长至关重要.
研究的目的:
- 为了确定BB0789.9的细胞质域的晶体结构.
- 阐明BB0789的ATPase和蛋白质分解活动的结构基础.
主要方法:
- 使用X射线晶体学来解决BB0789的结构166-614.
- 使用AlphaFold预测来建模中央孔隙区域.
- 生物化学分析证实了蛋白酶和ATPase活动.
主要成果:
- 晶体结构显示出一个由AAA+ ATPase和依赖的金属蛋白酶域组成的六米环.
- 在ADP-bound状态下观察到AAA+域.
- 蛋白酶域协调了一个离子,AlphaFold提供了缺少的中央孔的结构细节.
结论:
- BB0789形成一个功能性六合体,具有必要的ATPase和蛋白质分解活性.
- 对BB0789的结构洞察力可以更深入地了解它在Borrelia burgdorferi病原体中的作用.
- BB0789是针对莱姆病的治疗策略的验证目标.
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