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Atomic model of a myosin filament in the relaxed state

机译：松弛状态下肌球蛋白丝的原子模型

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摘要

Contraction of muscle involves the cyclic interaction of myosin heads on the thick filaments with actin subunits in the thin filaments(1). Muscles relax when this interaction is blocked by molecular switches on either or both filaments(2). Insight into the relaxed ( switched OFF) structure of myosin has come from electron microscopic studies of smooth muscle myosin molecules, which are regulated by phosphorylation. These studies suggest that the OFF state is achieved by an asymmetric, intramolecular interaction between the actin-binding region of one head and the converter region of the other, switching both heads off(3). Although this is a plausible model for relaxation based on isolated myosin molecules, it does not reveal whether this structure is present in native myosin filaments. Here we analyse the structure of a phosphorylation-regulated striated muscle thick filament using cryo-electron microscopy. Three-dimensional reconstruction and atomic fitting studies suggest that the 'interacting-head' structure is also present in the filament, and that it may underlie the relaxed state of thick filaments in both smooth and myosin-regulated striated muscles over a wide range of species.
机译：肌肉收缩涉及粗细丝上的肌球蛋白头部与细细丝中的肌动蛋白亚基的循环相互作用（1）。当这种相互作用被任一根或两条细丝上的分子开关阻断时，肌肉就会松弛（2）。对平滑肌肌球蛋白分子的电子显微镜研究已经深入了解了肌球蛋白的松弛（关闭）结构，平滑肌肌球蛋白分子受磷酸化作用调节。这些研究表明，OFF状态是通过一个头的肌动蛋白结合区域与另一个头的转化子区域之间的不对称分子内相互作用实现的，从而将两个头都关闭（3）。尽管这是基于分离的肌球蛋白分子的松弛的合理模型，但它并未揭示天然肌球蛋白丝中是否存在这种结构。在这里，我们使用低温电子显微镜分析磷酸化调节的横纹肌粗丝的结构。三维重建和原子拟合研究表明，细丝中也存在“相互作用头”结构，并且它可能是平滑细丝和肌球蛋白调节的横纹肌中厚丝的松弛状态的基础。

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