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Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue GltTk

Author

Listed:
  • Albert Guskov

    (University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute)

  • Sonja Jensen

    (University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute)

  • Ignacio Faustino

    (University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute)

  • Siewert J. Marrink

    (University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute
    University of Groningen, Zernike Institute for Advanced Materials)

  • Dirk Jan Slotboom

    (University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute
    University of Groningen, Zernike Institute for Advanced Materials)

Abstract

Glutamate transporters catalyse the thermodynamically unfavourable transport of anionic amino acids across the cell membrane by coupling it to the downhill transport of cations. This coupling mechanism is still poorly understood, in part because the available crystal structures of these transporters are of relatively low resolution. Here we solve crystal structures of the archaeal transporter GltTk in the presence and absence of aspartate and use molecular dynamics simulations and binding assays to show how strict coupling between the binding of three sodium ions and aspartate takes place.

Suggested Citation

  • Albert Guskov & Sonja Jensen & Ignacio Faustino & Siewert J. Marrink & Dirk Jan Slotboom, 2016. "Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue GltTk," Nature Communications, Nature, vol. 7(1), pages 1-6, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13420
    DOI: 10.1038/ncomms13420
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    Cited by:

    1. Zhenglai Zhang & Huiwen Chen & Ze Geng & Zhuoya Yu & Hang Li & Yanli Dong & Hongwei Zhang & Zhuo Huang & Juquan Jiang & Yan Zhao, 2022. "Structural basis of ligand binding modes of human EAAT2," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    2. Takafumi Kato & Tsukasa Kusakizako & Chunhuan Jin & Xinyu Zhou & Ryuichi Ohgaki & LiLi Quan & Minhui Xu & Suguru Okuda & Kan Kobayashi & Keitaro Yamashita & Tomohiro Nishizawa & Yoshikatsu Kanai & Osa, 2022. "Structural insights into inhibitory mechanism of human excitatory amino acid transporter EAAT2," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    3. Emanuela Colucci & Zaid R. Anshari & Miyer F. Patiño-Ruiz & Mariia Nemchinova & Jacob Whittaker & Dirk J. Slotboom & Albert Guskov, 2023. "Mutation in glutamate transporter homologue GltTk provides insights into pathologic mechanism of episodic ataxia 6," Nature Communications, Nature, vol. 14(1), pages 1-10, December.

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