在蛋白质farnesyltransferase中部位的结构特征
Daniel A Tobin1, Jennifer S Pickett, Heather L Hartman
1Department of Chemistry and Biophysics Research Division, The University of Michigan, Ann Arbor, MH 48109-1055, USA.
Journal of the American Chemical Society
|August 14, 2003
概括
射线吸收光谱学揭示了蛋白质法纳西尔转移酶中的 (Zn) 位点结构. 在基质结合时的结合变化,表明在酶的催化机制中发挥作用.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 频谱学是一种光谱学.
背景情况:
- 蛋白质法纳西转移酶 (FTase) 对于蛋白质前化至关重要.
- 了解 (Zn) 位点的结构和动态是阐明FTase的催化机制的关键.
研究的目的:
- 用X射线吸收光谱学确定FTase中的Zn位点结构.
- 调查基质结合如何影响 Zn 协调和 FTase 活性.
主要方法:
- 使用扩展的X射线吸收细结构 (EXAFS) 光谱学.
- 分析的重点是Zn-连接体距离和协调环境.
主要成果:
- EXAFS数据显示,Zn与三个低Z (N/O) 和一个囊硫原子结合.
- 在基质结合时,Zn协调保持四坐标,从ZnS(N/O) 3变为ZnS2(N/O) 2.
- 产品复合体的形成将 Zn 恢复到最初的 ZnS(N/O) 3 结合状态.
结论:
- 该研究提供了在FTase催化过程中Zn位点结构变化的光谱证据.
- 观察到的结合转移表明C端半氨酸在基质结合和催化中起作用.
- FTase的催化机制涉及到Zn协调球的动态变化.
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