Structure of Actin Filament and Mechanism of ATPase Activation upon Actin Assembly

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  • WAKABAYASHI Takeyuki
    Department of Biosciences, School of Science and Engineering; Department of Judo Therapy, Faculty of Medical Technology, Teikyo University
  • MURAKAMI Kenji
    Department of Biosciences, School of Science and Engineering; Department of Judo Therapy, Faculty of Medical Technology, Teikyo University

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Other Title
  • アクチンのフィラメント構造と重合機構―重合によるＡＴＰａｓｅ活性化のメカニズム―
  • アクチン ノ フィラメント コウゾウ ト ジュウゴウ キコウ : ジュウゴウ ニ ヨル ATPase カッセイカ ノ メカニズム

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Abstract

Actin assembly activates ATP hydrolysis, which provides structural cues for flament turnover. Polymerized actin supports cellular signaling, intracellular trafficking, and cytokinesis. We present the cryo-electron microscopic structure of F-actin in the presence of phosphate, with the visualization of some α-helical backbones and large side chains. A complete atomic model based on the cryo-EM identified intermolecular interactions, some of which were mediated by magnesium or phosphate ions. A critical role for bending of the proline-rich loop (residues 108-112) in activating ATPase was revealed. Crystal structures of G-actin mutants, which trap the catalytic site in two intermediate states, were solved. These structures combined with cryo-EM data allows us to propose a molecular mechanism for actin assembly and ATPase activation, critical for filament dynamics.<br>

Journal

  • Seibutsu Butsuri

    Seibutsu Butsuri 51 (6), 256-259, 2011

    The Biophysical Society of Japan General Incorporated Association

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