在Zymomonas mobilis pyruvate kinase的2.4 Å结构:对稳定性和调节的影响
Kathleen M Meneely1, Jeffrey S McFarlane2, Collette L Wright2
1Department of Chemistry, University of Texas at San Antonio, San Antonio, TX, 78249, USA.
Archives of biochemistry and biophysics
|July 2, 2023
概括
齐莫莫纳斯移动的酸盐激酶 (ZmPYK) 结构显示了酸盐离子,但没有全激活,与人类肝脏酸盐激酶 (hlPYK) 不同. ZmPYK可能缺乏基于效应者的活动监管的稳定性.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 酶学 是一种酶学.
背景情况:
- 人类肝脏酸盐激酶 (hlPYK) 是一种关键的甘油性酶,由果糖1,6-双酸盐 (FBP) 异质激活.
- 齐莫莫纳斯移动的酸激酶 (ZmPYK) 催化了Entner-Doudoroff通路的最后一步,缺乏FBP和全调节.
研究的目的:
- 阐明 ZmPYK 函数的结构基础.
- 通过将ZmPYK与hlPYK进行比较来研究ZmPYK潜在的全性调节机制.
主要方法:
- 进行X射线晶体学以确定ZmPYK的2.4 Å结构.
- 凝过色谱,以评估ZmPYK在溶液中的四元结构.
- 循环二极化 (CD) 光谱法用于评估蛋白质的热稳定性.
主要成果:
- 晶体结构显示ZmPYK是一种四聚体,与其二维溶液状态不同,与hlPYK相比,其四聚化接口较小.
- 一个酸盐离子被观察到与hlPYK中的FBP6酸盐结合部位相似的位置.
- CD化曲线显示ZmPYK和hlPYK之间的热稳定性没有显著差异,除了ZmPYK曲线中的一个微小的额外阶段.
结论:
- 在测试条件下,酸盐离子在ZmPYK中似乎没有发挥结构性或性作用.
- ZmPYK很可能缺乏必要的蛋白质稳定性,使其活性受到全效应因子的调节,与其人类同类不同.
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