Structure and Dynamics of Membrane-embedded KcsA Potassium Channel Revealed by Atomic Force Microscopy

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  • SUMINO Ayumi
    Department of Molecular Physiology and Biophysics, Faculty of Medical Sciences, University of Fukui PRESTO, Japan Science and Technology Agency (JST)
  • YAMAMOTO Daisuke
    Department of Applied Physics, Fukuoka University
  • SUMIKAMA Takashi
    Department of Molecular Physiology and Biophysics, Faculty of Medical Sciences, University of Fukui
  • IWAMOTO Masayuki
    Department of Molecular Physiology and Biophysics, Faculty of Medical Sciences, University of Fukui
  • DEWA Takehisa
    Department of Frontier Materials, Graduate School of Engineering, Nagoya Institute of Technology
  • OIKI Shigetoshi
    Department of Molecular Physiology and Biophysics, Faculty of Medical Sciences, University of Fukui

Bibliographic Information

Other Title
  • 膜内KcsAカリウムチャネルの原子間力顕微鏡による構造と動態解析
  • マク ナイ KcsA カリウムチャネル ノ ゲンシ カンリョク ケンビキョウ ニ ヨル コウゾウ ト ドウタイ カイセキ

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Abstract

The KcsA channel is a prototypical potassium channel, exhibiting pH-dependent gating. The structure of the transmembrane pore-domain of the KcsA channel was examined using atomic force microscopy (AFM) under the membrane-embedded condition. In the closed conformation, the cytoplasmic end of the pore domain was protruded from the membrane surface. In the open conformation, the open pore at the center of the tetrameric channel was resolved, and the protrusion was substantially shortened relative to the closed conformation. High-speed AFM revealed the clustering–dispersion dynamics upon pH changes, and this collective behavior was closely related to the gating conformational changes.

Journal

  • Seibutsu Butsuri

    Seibutsu Butsuri 55 (1), 005-010, 2015

    The Biophysical Society of Japan General Incorporated Association

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