多域氧传感器DosP的结构:通过调节性PAS域的远程控制c-di-GMP二酶
Wenbi Wu1, Pankaj Kumar1, Chad A Brautigam2,3
1Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
bioRxiv : the preprint server for biology
|August 2, 2024
概括
细菌酶DosP降解了循环-di-GMP (c-di-GMP). 这是一种细菌酶. 氧气与DosP结合在一起.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 微生物学 微生物学
背景情况:
- DosP 是大肠杆菌中一种基于血红素的传感蛋白.
- 它降解了循环-di-GMP (c-di-GMP),一种细菌的第二信使.
- 氧的结合可以全osterically 增强DosP的固酶活性.
研究的目的:
- 通过DosP阐明氧介导c-di-GMP降解的全质性机制.
- 为了确定DosP在氧气和基质结合时的结构变化的结构基础.
主要方法:
- 全长DosP的X射线晶体学 (确定了六个结构).
- 生物化学试验用于研究酶活性和基质结合.
- 位点定向的突变发生来探测蛋白质的功能.
主要成果:
- DosP存在于一个长长的二元体中,和固酶域空间分离.
- 在没有基质的情况下,DosP采用了两种形状的平衡.
- 基质结合锁定DosP成一个ON或OFF状态的形状,取决于血氧化状态.
结论:
- 结构和生化数据揭示了DosP通过氧气的全调节.
- 氧结合通过形状控制调节c-di-GMP第二信使水平.
- 对细菌信号和酶调节机制的洞察.
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