Molecular architecture of the KvAP voltage-dependent K+ channel in a lipid bilayer
Molecular architecture of the KvAP voltage-dependent K+ channel in a lipid bilayer
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DOI：
10.1126/science.1101373
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发表时间：
2004-10-15
期刊：
影响因子：
56.9
通讯作者：
Perozo, E
中科院分区：
文献类型：
--
作者：
Cuello, LG;Cortes, DM;Perozo, E
我们利用定点自旋标记和电子顺磁共振波谱技术，分析了在0毫伏时原核生物电压依赖性K⁺通道（KvAP）的局部结构和动力学。我们表明，S4片段位于蛋白质/脂质界面，其大部分电荷受到保护，不与脂质环境接触。在结构上，S4具有高度的动态性，并通过一个柔性连接体被分隔成两个短螺旋。可及性和动力学数据表明，S1片段被蛋白质的其他部分所包围。我们提出，S1位于电压感应结构域和孔结构域之间的接触界面。这些结果确立了生物膜中电压依赖性通道结构的一般原理。
We have analyzed the local structure and dynamics of the prokaryotic voltage-dependent K+ channel (KvAP) at 0 millivolts, using site-directed spin labeling and electron paramagnetic resonance spectroscopy. We show that the S4 segment is located at the protein/lipid interface, with most of its charges protected from the lipid environment. Structurally, S4 is highly dynamic and is separated into two short helices by a flexible linker. Accessibility and dynamics data indicate that the S1 segment is surrounded by other parts of the protein. We propose that S1 is at the contact interface between the voltage-sensing and pore domains. These results establish the general principles of voltage-dependent channel structure in a biological membrane.