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在MAS NMR中的Peroxiredoxin中引起的二硫化键结构挫折和动态障碍

Laura Troussicot^1,2,3,4, Alicia Vallet³, Mikael Molin^1,5

¹Department of Chemistry and Molecular Biology, University of Gothenburg, SE-405 30 Göteborg, Sweden.

Journal of the American Chemical Society

|May 4, 2023

概括

蛋白质二硫化键的形成驱动了多氧化 (PRDX) 的动态结构变化,揭示了它们的伴侣功能和细胞调节的洞察力. 这项研究揭示了与结构丧相关的μs时间尺度动态.

科学领域:

生物化学和分子生物学
蛋白质动力学和结构
细胞再氧化调节

背景情况:

二硫化键对于蛋白质结构和细胞内氧化状态的调节至关重要.
过氧素 (PRDXs) 通过一种涉及囊氧化和还原的催化循环来排毒活性氧物种.
在囊氧化后,PRDXs会发生构造变化,包括寡合化,可能会调解伴侣功能.

研究的目的:

研究二硫化物键形成对PRDX的动态的影响.
阐明PRDX的结构基础.
了解PRDX中的形状重组的时间范围和性质.

主要方法:

在216kDa的Tsa1数组上进行神奇角旋转 (MAS) 核磁共振光谱.
在设计的二度PRDX突变体上进行溶液NMR光谱.
在微秒 (μs) 时间尺度上分析蛋白质动态.

主要成果:

在PRDX催化周期中,二硫化物键的形成诱导了广泛的μs时间尺度动态.
在大型的decameric和设计的二维PRDX组件中观察到一致的动态.
这些动态归因于结构上的挫折,

结论:

在PRDX中形成二硫化键是重要的蛋白质动态的关键驱动因素.
结构挫折解释了尽管存在二硫化物键约束,但观察到的形状灵活性.
这些发现为了解PRDX在氧化还原调节和分子监护中的作用提供了结构基础.

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