通过Legionella效应体SdeA对ubiquitin的修饰的结构基础
Yanan Dong1, Yajuan Mu1, Yongchao Xie1
1Beijing Advanced Innovation Center for Soft Matter Science and Engineering, Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, China.
Nature
|May 26, 2018
概括
这项研究揭示了Legionella SdeA背后的结构机制
科学领域:
- 分子生物学
- 结构生物学
- 生物化学
背景情况:
- 蛋白质无化是一种关键的翻译后修饰,可以调节真核细胞过程.
- 菌效应剂SdeA调解一种独特的基联泛化,但其机制尚不清楚.
研究的目的:
- 阐明SdeA介导的泛胺修饰的结构机制.
- 了解基联泛化过程.
主要方法:
- 使用X射线结晶学来确定SdeA在各种状态中的结构 (无体,Ub结合,Ub-NADH结合).
- 在Ubiquitin结合时SdeA的形状变化的分析.
主要成果:
- 这些结构表明SdeA的单-ADP-ribosyltransferase (mART) 和基酶 (PDE) 域形成了催化域.
- 在mART域的ARTT和PN循环中诱导显著的形状变化.
- 在ADP-ribosylation过程中,Ubiquitin的Arg72可以作为探针,启动相互作用和随后的侧链运动.
结论:
- 这项研究提供了SdeA介导的基修饰的结构性见解.
- 这项工作为进一步研究基联无处不在机制奠定了基础.
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