R
Ryosuke Nakashima
Researcher at Osaka University
Publications - 25
Citations - 6062
Ryosuke Nakashima is an academic researcher from Osaka University. The author has contributed to research in topics: Cytochrome c oxidase & Drug export. The author has an hindex of 15, co-authored 22 publications receiving 5702 citations.
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Journal ArticleDOI
The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A.
Tomitake Tsukihara,Hiroshi Aoyama,Eiki Yamashita,Takashi Tomizaki,Hiroshi Yamaguchi,Kyoko Shinzawa-Itoh,Ryosuke Nakashima,Rieko Yaono,Shinya Yoshikawa +8 more
TL;DR: Two possible proton pathways for pumping, each spanning from the matrix to the cytosolic surfaces, were identified, including hydrogen bonds, internal cavities likely to contain water molecules, and structures that could form hydrogen bonds with small possible conformational change of amino acid side chains.
Journal ArticleDOI
Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A
Tomitake Tsukihara,Hiroshi Aoyama,Eiki Yamashita,Takashi Tomizaki,Hiroshi Yamaguchi,Kyoko Shinzawa-Itoh,Ryosuke Nakashima,Rieko Yaono,Shinya Yoshikawa +8 more
TL;DR: The high resolution three-dimensional x-ray structure of the metal sites of bovine heart cytochrome c oxidase is reported, suggesting a dinuclear copper center with an unexpected structure similar to a [2Fe-2S]-type iron-sulfur center.
Journal ArticleDOI
Crystal structure of bacterial multidrug efflux transporter AcrB
TL;DR: In this article, the crystal structure of AcrB at 3.5 A resolution was determined, which implies that substrates translocated from the cell interior through the transmembrane region and from the periplasm through the vestibules are collected in the central cavity and then actively transported through the pore into the TolC tunnel.
Journal ArticleDOI
Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
TL;DR: AcrB as discussed by the authors is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA.
Journal ArticleDOI
Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket
TL;DR: The crystal structures of AcrB bound to the high-molecular-mass drugs rifampicin and erythromycin indicate that there are two discrete multisite binding pockets along the intramolecular channel.