Structural Basis for Dynamic Mechanism of Proton-Coupled Symport by the Peptide Transporter POT

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  • ISHITANI Ryuichiro
    Department of Biophysics and Biochemistry, Graduate School of Science, the University of Tokyo
  • DOKI Shintaro
    Department of Biophysics and Biochemistry, Graduate School of Science, the University of Tokyo
  • KATO Hideaki E.
    Department of Biophysics and Biochemistry, Graduate School of Science, the University of Tokyo
  • NUREKI Osamu
    Department of Biophysics and Biochemistry, Graduate School of Science, the University of Tokyo

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  • X線結晶構造解析と分子動力学シミュレーションで紐解く膜輸送体の分子機構
  • Xセン ケッショウ コウゾウ カイセキ ト ブンシ ドウリキガク シミュレーション デ ヒモトク マク ユソウタイ ノ ブンシ キコウ

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Abstract

Membrane transporters transport their substrates across the membrane, thereby contributing to the maintenance of the cellular environments. One of the largest superfamily of the membrane transporters is Major Facilitator Superfamily (MFS), and many of MFS transporters are involved in the cellular uptake of various compounds utilizing the proton motive force across the membrane. Although several crystal structures of MFS transporters have been reported so far, their active transport mechanism has still remained elusive. Proton-dependent oligopeptide transporter, POT, is a member of MFS, and is involved in the uptake of oligopeptides as well as peptide-like drugs. In this article, we explain the active transporter mechanism by POT based on our recent results of the structural and computational analyses.<br>

Journal

  • Seibutsu Butsuri

    Seibutsu Butsuri 54 (2), 085-090, 2014

    The Biophysical Society of Japan General Incorporated Association

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