与AMP-PNP结合的维生素B12载体BtuCD-F的结构
Vladimir M Korkhov1, Samantha A Mireku, Kaspar P Locher
1Institute of Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland.
Nature
|September 25, 2012
概括
对于大肠杆菌中维生素B12吸收至关重要的ATP结合盒 (ABC) 运输体BtuCD,揭示了一种新的运输机制. 结构和功能研究揭示了一个独特的中间状态和围静运动,与其他ABC传送器不同.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 微生物学 微生物学
背景情况:
- ATP结合盒 (ABC) 载体BtuCD促进大肠杆菌的维生素B12吸收.
- 之前的结构研究阐明了阿波状态,但没有阐明运输机制.
研究的目的:
- 通过确定一个功能中间状态的结构来阐明BtuCD的传输机制.
主要方法:
- 3.5 Å结晶结构确定与AMP-PNP结合的BtuCD-BtuF复合体.
- 放射性合物捕获试验. 放射性合物捕获试验.
- 工程二硫化物交叉连接和功能测试.
主要成果:
- BtuC子单元的新型构造揭示了一个密封的细胞质门,形成了一个封闭的腔.
- 这种位于膜中间的空洞容纳了维生素B12.
- 在AMP-PNP的存在下,BtuCD-F复合体与维生素B12结合.
结论:
- 这些发现表明,维生素B12有意想不到的环静脉运输机制.
- 这种机制与在其他ABC传送器中观察到的机制有很大不同.
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