PH0140的晶体结构:外源氨基酸诱导开放的八元组合使促进者TTTT 绑定转录调节
Richard Mariadasse1, Mohammed Ahmad2, Ravi Kant Pal2
1Department of Bioinformatics, Alagappa University, Tamil Nadu, India; Department of Neurology, Yale University, School of Medicine, USA.
Journal of molecular biology
|February 3, 2026
概括
Pyrococcus horikoshii PH0140 蛋白质与异黄素和酸盐结合,揭示了其结构和转录调节机制. 这项研究阐明了宴会/饥荒调节蛋白家族成员如何与DNA相互作用.
科学领域:
- 微生物学 微生物学
- 结构生物学 结构生物学
- 分子生物学分子生物学
背景情况:
- PH0140是一种来自Pyrococcus horikoshii OT3中Feast/Famine Regulatory Protein (FFRP) 家族的假设蛋白质,它与转录调节有关.
- 之前的in-silico研究表明PH0140通过DNA识别和全ostery结合和调节转录,但其结构和机制是未知的.
研究的目的:
- 为了确定PH0140.0.的晶体结构.
- 阐明PH0140在对外源氨基酸的反应中的调节机制.
- 为了研究连接体结合和DNA相互作用的结构基础.
主要方法:
- 进行X射线晶体学以确定PH0140结构.
- 尺寸排除色谱用于评估寡合化.
- 异热定位热量计 (ITC) 用于氨基酸结合分析.
- PH0140-DNA复合体的分子动力学模拟.
主要成果:
- PH0140的晶体结构透露了通过独特的C端环和偏离的β链 (β4) 与异黄素的结合.
- 在异黄素和氨酸的存在下,PH0140形成寡合物,而氨酸具有更高的结合亲和力.
- 分子动力学模拟显示,八米基PH0140经历着构造性开放,与DNA促进体TTTT区域相互作用.
结论:
- PH0140的结构和寡合化是由外源氨基酸调节的,特别是托.
- 蛋白质通过疏水性相互作用采用开放形状,促进DNA促进体结合以进行转录调节.
- 这项研究为FFRP家族的转录控制机制提供了结构性的见解.
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