Ion Mobility Mass Spectrometry of Two Tetrameric Membrane Protein Complexes Reveals Compact Structures and Differences in Stability and Packing
Ion Mobility Mass Spectrometry of Two Tetrameric Membrane Protein Complexes Reveals Compact Structures and Differences in Stability and Packing
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DOI：
10.1021/ja104312e
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发表时间：
2010-11-10
影响因子：
15
通讯作者：
Robinson, Carol V.
中科院分区：
文献类型：
--
作者：
Wang, Sheila C.;Politis, Argyris;Robinson, Carol V.
在这里，我们研究了气相结构的两个四聚体膜蛋白复合物的离子迁移质谱。离子通道测量的碰撞截面与亚基的紧凑配置雅阁，表明在将其从洗涤剂胶束释放到气相中所需的苛刻活化条件下，可以保留天然样结构。我们还发现，转运蛋白的四级结构，它具有较少的跨膜亚基比离子通道，是不太稳定，一旦剥离洗涤剂和散装水。这些结果突出了潜在的离子迁移质谱表征膜蛋白复合物的整体拓扑结构和结构变化与核苷酸，脂质和药物结合。
Here we examined the gas-phase structures of two tetrameric membrane protein complexes by ion mobility mass spectrometry. The collision cross sections measured for the ion channel are in accord with a compact configuration of subunits, suggesting that the native-like structure can be preserved under the harsh activation conditions required to release it from the detergent micelle into the gas phase. We also found that the quaternary structure of the transporter, which has fewer transmembrane subunits than the ion channel, is less stable once stripped of detergents and bulk water. These results highlight the potential of ion mobility mass spectrometry for characterizing the overall topologies of membrane protein complexes and the structural changes associated with nucleotide, lipid, and drug binding.