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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