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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Allostery of actin filaments: Molecular dynamics simulations and coarse-grained analysis
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Allostery of actin filaments: Molecular dynamics simulations and coarse-grained analysis

机译：肌动蛋白丝的变构：分子动力学模拟和粗粒度分析

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摘要

The structural and mechanical properties of monomeric actin (G-actin), the trimer nucleus, and actin filaments (F-actins) are determined as a function of the conformation of the DNase I-binding loop (DB loop) by using all-atom molecular dynamics simulations and coarse-grained (CG) analysis. Recent x-ray structures of ADP-bound G-actin (G-ADP) by Otterbein et al. and ATP-bound G-actin (G-ATP) by Graceffa and Dominguez indicate that the DB loop of actin does not have a well defined secondary structure in the ATP state but folds into an a-helix in the ADP state. MD simulations and CG analysis indicate that such a helical DB loop significantly weakens the intermonomer interactions of actin assemblies and thus leads to a wider, shorter, and more disordered filament. The computed persistence lengths of F-actin composed of G-ATP (16 mu m) and of G-ADP (8.5 mu m) agree well with the experimental values for the two states. Therefore, the loop-to-helix transition of the DB loop may be one of the factors that lead to the changes in structural and mechanical properties of F-actin after ATP hydrolysis. This result may provide a direct connection between the conformational changes of an actin monomer and the structural and mechanical properties of the cytoskeleton. The information provided by MID simulations also helps to understand the possible origin of the special features of actin dynamics.
机译：单体肌动蛋白（G-肌动蛋白），三聚体核和肌动蛋白丝（F-肌动蛋白）的结构和力学性质是通过使用全原子确定的，取决于DNase I结合环（DB环）的构象分子动力学模拟和粗粒度（CG）分析。 Otterbein等人最近研究了ADP结合的G-肌动蛋白（G-ADP）的X射线结构。 Graceffa和Dominguez的ATP结合G-肌动蛋白（G-ATP）表明，肌动蛋白的DB环在ATP状态下没有明确定义的二级结构，但在ADP状态下折叠成a-螺旋。 MD模拟和CG分析表明，这种螺旋DB环显着削弱了肌动蛋白组件的单体间相互作用，从而导致丝线更宽，更短和更无序。由G-ATP（16μm）和G-ADP（8.5μm）组成的F-肌动蛋白的持久性长度与两种状态的实验值吻合良好。因此，DB环的从环到螺旋的转变可能是导致ATP水解后F-肌动蛋白的结构和机械性质发生变化的因素之一。该结果可以提供肌动蛋白单体的构象变化与细胞骨架的结构和机械性质之间的直接联系。 MID模拟提供的信息还有助于了解肌动蛋白动力学特殊特征的可能来源。

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