来自G. acetivorans的RNA激酶ArK1的高分辨率晶体结构
Chulei Cao1, Weizhen Zhang1, Yanqing Gao1
1Shanghai Sci-Tech Inno Center for Infection & Immunity, State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Biochemistry and Biophysics, School of Life Sciences, Fudan University, Shanghai, 200438, PR China.
Biochemical and biophysical research communications
|April 24, 2024
概括
古代RNA激酶 (Ark1) 结合ATP,这是tRNA修饰的关键步骤. 对GaArk1的结构分析显示,在同类蛋白质中保留了ATP结合机制.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 分子生物学分子生物学
背景情况:
- U47酸化 (Up47) 是最近发现的一种增强tRNA稳定性和抗性的tRNA修饰.
- 古代RNA激酶 (Ark1) 以ATP依赖的方式催化Up47,但其基质结合机制仍然未知.
研究的目的:
- 为了阐明由Archaeal RNA激酶 (Ark1) 结合ATP的结构基础.
- 描述来自G. acetivorans (GaArk1) 的Ark1蛋白及其与ATP的相互作用.
主要方法:
- 对GaArk1.1的表达和净化
- 在Apo形式的GaArk1的结晶,并与ATP复合.
- 为GaArk1-ATP复合体确定原子分辨率结构.
主要成果:
- 确定了GaArk1-ATP复合体的晶体结构,提供了Ark1蛋白中ATP结合的第一个原子层次视图.
- 鉴定了参与ATP结合的保存残留物,这表明Ark1同类物中存在保存结合机制.
- 序列和结构分析显示,瓜诺辛抑制了特定的Ark1蛋白.
结论:
- 确定的GaArk1-ATP结构揭示了Ark1对ATP结合的详细机制.
- 保存的ATP结合残留物表明在同类Ark1蛋白中存在一个共同的机制.
- 瓜诺辛对某些Ark1酶表现出特定的抑制作用.
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