High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism.
High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism.
复制标题
肌动球蛋白-V复合物在三种核苷酸状态下的高分辨率结构提供了对力产生机制的见解。
DOI：
10.7554/elife.73724
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发表时间：
2021-11-23
期刊：
影响因子：
7.7
通讯作者：
Raunser S
中科院分区：
文献类型：
--
作者：
Pospich S;Sweeney HL;Houdusse A;Raunser S
分子马达肌球蛋白在其产生力的马达周期中经历一系列主要的结构转变。基本的机制及其耦合ATP水解和肌动蛋白结合只有部分了解，主要是由于稀疏的结构数据肌动蛋白结合状态的肌球蛋白。在这里，我们报告了26个高分辨率的cryo-EM结构的肌动球蛋白-V复杂的强ADP，僵硬，和以前看不见的僵硬后过渡状态，结合ATP类似物AppNHP。这些结构揭示了肌球蛋白在每种状态下的高灵活性，并提供了有价值的见解肌球蛋白-V ADP释放和AppNHP结合后的结构转变，以及肌动球蛋白接口。此外，他们还展示了肌球蛋白如何能够特异性地改变F-肌动蛋白的结构。
The molecular motor myosin undergoes a series of major structural transitions during its force-producing motor cycle. The underlying mechanism and its coupling to ATP hydrolysis and actin binding are only partially understood, mostly due to sparse structural data on actin-bound states of myosin. Here, we report 26 high-resolution cryo-EM structures of the actomyosin-V complex in the strong-ADP, rigor, and a previously unseen post-rigor transition state that binds the ATP analog AppNHp. The structures reveal a high flexibility of myosin in each state and provide valuable insights into the structural transitions of myosin-V upon ADP release and binding of AppNHp, as well as the actomyosin interface. In addition, they show how myosin is able to specifically alter the structure of F-actin.