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Structural basis for amino acid export by DMT superfamily transporter YddG

Author

Listed:
  • Hirotoshi Tsuchiya

    (Graduate School of Science, The University of Tokyo)

  • Shintaro Doki

    (Graduate School of Science, The University of Tokyo)

  • Mizuki Takemoto

    (Graduate School of Science, The University of Tokyo)

  • Tatsuya Ikuta

    (Graduate School of Science, The University of Tokyo)

  • Takashi Higuchi

    (Graduate School of Science, The University of Tokyo)

  • Keita Fukui

    (Research Institute for Bioscience Products & Fine Chemicals, Ajinomoto Co., Inc.)

  • Yoshihiro Usuda

    (Institute for Innovation, Ajinomoto Co., Inc.)

  • Eri Tabuchi

    (Institute for Innovation, Ajinomoto Co., Inc.)

  • Satoru Nagatoishi

    (School of Engineering, The University of Tokyo)

  • Kouhei Tsumoto

    (School of Engineering, The University of Tokyo)

  • Tomohiro Nishizawa

    (Graduate School of Science, The University of Tokyo)

  • Koichi Ito

    (Graduate School of Frontier Sciences, The University of Tokyo)

  • Naoshi Dohmae

    (Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science)

  • Ryuichiro Ishitani

    (Graduate School of Science, The University of Tokyo
    Theoretical Molecular Science Laboratory, RIKEN)

  • Osamu Nureki

    (Graduate School of Science, The University of Tokyo)

Abstract

The X-ray structure of the drug/metabolite transporter (DMT) protein YddG from Starkeya novella reveals a new membrane transport topology, with ten transmembrane segments in an outward-facing state and two pseudo-symmetric inverted structural repeats.

Suggested Citation

  • Hirotoshi Tsuchiya & Shintaro Doki & Mizuki Takemoto & Tatsuya Ikuta & Takashi Higuchi & Keita Fukui & Yoshihiro Usuda & Eri Tabuchi & Satoru Nagatoishi & Kouhei Tsumoto & Tomohiro Nishizawa & Koichi , 2016. "Structural basis for amino acid export by DMT superfamily transporter YddG," Nature, Nature, vol. 534(7607), pages 417-420, June.
  • Handle: RePEc:nat:nature:v:534:y:2016:i:7607:d:10.1038_nature17991
    DOI: 10.1038/nature17991
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