Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein
Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein
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DOI：
10.1038/nmeth.2635
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发表时间：
2013-10-01
期刊：
影响因子：
48
通讯作者：
Ladizhansky, Vladimir
中科院分区：
文献类型：
--
作者：
Wang, Shenlin;Munro, Rachel A.;Ladizhansky, Vladimir
确定完整膜蛋白的结构，尤其是在其天然环境中，是结构生物学中的一项艰巨挑战。在这里，我们证明魔角旋转固态核磁共振波谱可用于确定在合成脂质（类似于天然膜的环境）中重建的膜蛋白的结构。我们结合大量实验确定的原子间距离和局部扭转约束来解决常见七螺旋折叠寡聚膜蛋白鱼腥藻感觉视紫红质（ASR）的结构。我们确定了 ASR 三聚体寡聚界面的原子分辨率细节，以及单体中螺旋、侧链和视网膜辅因子的排列。
Determination of structure of integral membrane proteins, especially in their native environment, is a formidable challenge in structural biology. Here we demonstrate that magic angle spinning solid-state NMR spectroscopy can be used to determine structures of membrane proteins reconstituted in synthetic lipids, an environment similar to the natural membrane. We combined a large number of experimentally determined interatomic distances and local torsional restraints to solve the structure of an oligomeric membrane protein of common seven-helical fold, Anabaena sensory rhodopsin (ASR). We determined the atomic resolution detail of the oligomerization interface of the ASR trimer, and the arrangement of helices, side chains and the retinal cofactor in the monomer.