NAD+消耗蛋白 Acinetobacter baumannii TIR 域的结构显示出独特的动力学和形状
Erik Klontz1, Juliet O Obi2, Yajing Wang3
1Division of Vaccine Research, Institute of Human Virology, School of Medicine, University of Maryland, Baltimore, Maryland, USA.
The Journal of biological chemistry
|September 27, 2023
概括
Acinetobacter baumannii TIR 蛋白质对NAD+进行水解,这一过程对细菌信号传递至关重要. 结构和成像研究显示了基质诱导的构造变化,影响了细菌的功能.
科学领域:
- 生物化学和分子生物学
- 结构生物学 结构生物学
- 微生物学 微生物学
背景情况:
- 托尔类和介质素-1/18受体/抗性 (TIR) 域蛋白质是关键的信号和免疫调节剂.
- TIR蛋白质在各种生物体中具有NAD+酶活性,包括细菌,植物和哺乳动物.
研究的目的:
- 为了阐明Acinetobacter baumannii TIR域蛋白 (AbTir-TIR) 的晶体结构.
- 为了研究NAD+与AbTir-TIR结合的结构效应.
- 通过使用先进的成像技术,探索AbTir-TIR的NAD+酶活性对生物学的相关性.
主要方法:
- 进行X射线晶体学以确定AbTir-TIR结构.
- -交换质谱法 (HDX-MS) 用于绘制NAD+相互作用的形状变化.
- 用光终身成像显微镜 (2PE-FLIM) 激发2光子,用于无标签的细菌成像.
主要成果:
- 确定了AbTir-TIR的晶体结构,证实了它的NAD+水解能力.
- 结合NAD+在二维接口上诱导了微妙的构造变化,EX1动力学表明了大的合作转移.
- 基质结合减缓了这些构造变化;成像显示了细菌中原生和突变的AbTir-TIR之间的差异.
结论:
- 基质诱导的构造变化是细菌TIR蛋白与NAD+酶活性机制的组成部分.
- 这些发现增强了对细菌TIR蛋白功能及其多样化的生物作用的理解.
- 该研究提供了对关键细菌酶的结构和功能见解.
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