An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation.
An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation.
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DOI：
10.1085/jgp.200910376
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发表时间：
2010-10
期刊：
影响因子：
--
通讯作者：
Martinac B
中科院分区：
文献类型：
--
作者：
Corry B;Hurst AC;Pal P;Nomura T;Rigby P;Martinac B
机械敏感性通道作为施加在活细胞膜上的机械力的分子换能器，通过响应于在生理过程如触觉、听觉、血压调节和呼吸调节中发生的膜双层变形而打开。在这里，我们确定了可能的结构的开放状态的机械敏感通道的大电导使用膜片钳，荧光共振能量转移（FRET）光谱，数据从以前的电子顺磁共振实验，分子和布朗动力学模拟的组合。我们表明，结构重排的蛋白质可以测量在类似的条件下，膜片钳记录，同时控制状态的孔在其天然脂质环境中通过修改的侧向压力分布通过脂质双层。向开放状态的转变没有以前提出的那么引人注目，而N末端仍然锚定在膜的表面，在那里它可以引导膜张力的倾斜或直接将膜张力转化为孔衬螺旋的构象。结合FRET在生理条件下获得的数据与模拟可能是研究在一系列的多聚体膜蛋白的构象变化具有很大的价值。
Mechanosensitive channels act as molecular transducers of mechanical force exerted on the membrane of living cells by opening in response to membrane bilayer deformations occurring in physiological processes such as touch, hearing, blood pressure regulation, and osmoregulation. Here, we determine the likely structure of the open state of the mechanosensitive channel of large conductance using a combination of patch clamp, fluorescence resonance energy transfer (FRET) spectroscopy, data from previous electron paramagnetic resonance experiments, and molecular and Brownian dynamics simulations. We show that structural rearrangements of the protein can be measured in similar conditions as patch clamp recordings while controlling the state of the pore in its natural lipid environment by modifying the lateral pressure distribution via the lipid bilayer. Transition to the open state is less dramatic than previously proposed, while the N terminus remains anchored at the surface of the membrane where it can either guide the tilt of or directly translate membrane tension to the conformation of the pore-lining helix. Combining FRET data obtained in physiological conditions with simulations is likely to be of great value for studying conformational changes in a range of multimeric membrane proteins.
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