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首页> 外文期刊>Journal of Molecular Biology >Three-dimensional architecture of membrane-embedded MscS in the closed conformation
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Three-dimensional architecture of membrane-embedded MscS in the closed conformation

机译：膜包埋的MscS处于封闭构象的三维结构

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摘要

The mechanosensitive channel of small conductance (MscS) is part of a coordinated response to osmotic challenges in Escherichia coli. MscS opens as a result of membrane tension changes, thereby releasing small solutes and effectively acting as an osmotic safety valve. Both the functional state depicted by its crystal structure and its gating mechanism remain unclear. Here, we combine site-directed spin labeling, electron paramagnetic resonance spectroscopy, and molecular dynamics simulations with novel energy restraints based on experimental electron paramagnetic resonance data to investigate the native transmembrane (TM) and periplasmic molecular architecture of closed MscS in a lipid bilayer. In the closed conformation, MscS shows a more compact TM domain than in the crystal structure, characterized by a realignment of the TM segments towards the normal of the membrane. The previously unresolved NH2-terminus forms a short helical hairpin capping the extracellular ends of TM1 and TM2 and is in close interaction with the bilayer interface. The present three-dimensional model of membrane-embedded MscS in the closed state represents a key step in determining the molecular mechanism of MscS gating.
机译：小电导（MscS）的机械敏感通道是大肠杆菌对渗透挑战的协调响应的一部分。由于膜张力的变化，MscS打开，从而释放出少量溶质，并有效地充当了渗透安全阀。由其晶体结构和其门控机制描绘的功能状态仍然不清楚。在这里，我们结合定点自旋标记，电子顺磁共振光谱学和分子动力学模拟与基于实验电子顺磁共振数据的新型能量约束条件，以研究脂质双层中封闭MscS的天然跨膜（TM）和周质分子结构。在闭合构象中，MscS显示出比晶体结构更紧密的TM结构域，其特征在于TM片段朝着膜的法线方向重新排列。先前未解析的NH2-末端形成一个短的螺旋发夹，覆盖着TM1和TM2的细胞外末端，并与双层界面紧密相互作用。目前处于封闭状态的膜嵌入MscS的三维模型代表了确定MscS门控分子机制的关键步骤。

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