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Structural basis for ion selectivity revealed by high-resolution crystal structure of Mg2+ channel MgtE

Author

Listed:
  • Hironori Takeda

    (Graduate School of Science, University of Tokyo
    Global Research Cluster, RIKEN)

  • Motoyuki Hattori

    (Graduate School of Science, University of Tokyo
    Global Research Cluster, RIKEN
    Precursory Research for Embryonic Science and Technology (PRESTO), Japan Science and Technology Agency
    School of Life Sciences, Fudan University)

  • Tomohiro Nishizawa

    (Graduate School of Science, University of Tokyo
    Global Research Cluster, RIKEN)

  • Keitaro Yamashita

    (SR Life Science Instrumentation Unit, RIKEN SPring-8 Center)

  • Syed T. A. Shah

    (Membrane Structural and Functional Biology Group, School of Medicine, and School of Biochemistry and Immunology, Trinity College Dublin)

  • Martin Caffrey

    (Membrane Structural and Functional Biology Group, School of Medicine, and School of Biochemistry and Immunology, Trinity College Dublin)

  • Andrés D. Maturana

    (Graduate School of Bioagricultural Sciences, Nagoya University)

  • Ryuichiro Ishitani

    (Graduate School of Science, University of Tokyo
    Global Research Cluster, RIKEN)

  • Osamu Nureki

    (Graduate School of Science, University of Tokyo
    Global Research Cluster, RIKEN)

Abstract

Magnesium is the most abundant divalent cation in living cells and is crucial to several biological processes. MgtE is a Mg2+ channel distributed in all domains of life that contributes to the maintenance of cellular Mg2+ homeostasis. Here we report the high-resolution crystal structures of the transmembrane domain of MgtE, bound to Mg2+, Mn2+ and Ca2+. The high-resolution Mg2+-bound crystal structure clearly visualized the hydrated Mg2+ ion within its selectivity filter. Based on those structures and biochemical analyses, we propose a cation selectivity mechanism for MgtE in which the geometry of the hydration shell of the fully hydrated Mg2+ ion is recognized by the side-chain carboxylate groups in the selectivity filter. This is in contrast to the K+-selective filter of KcsA, which recognizes a dehydrated K+ ion. Our results further revealed a cation-binding site on the periplasmic side, which regulate channel opening and prevents conduction of near-cognate cations.

Suggested Citation

  • Hironori Takeda & Motoyuki Hattori & Tomohiro Nishizawa & Keitaro Yamashita & Syed T. A. Shah & Martin Caffrey & Andrés D. Maturana & Ryuichiro Ishitani & Osamu Nureki, 2014. "Structural basis for ion selectivity revealed by high-resolution crystal structure of Mg2+ channel MgtE," Nature Communications, Nature, vol. 5(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6374
    DOI: 10.1038/ncomms6374
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