Structural basis for amino acid export by DMT superfamily transporter YddG

Hirotoshi Tsuchiya, Shintaro Doki, Mizuki Takemoto, Tatsuya Ikuta, Takashi Higuchi, Keita Fukui, Yoshihiro Usuda, Eri Tabuchi, Satoru Nagatoishi, Kouhei Tsumoto, Tomohiro Nishizawa, Koichi Ito, Naoshi Dohmae, Ryuichiro Ishitani () and Osamu Nureki ()
Additional contact information
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
Osamu Nureki: Graduate School of Science, The University of Tokyo

Nature, 2016, vol. 534, issue 7607, 417-420

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.

Date: 2016
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DOI: 10.1038/nature17991

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