Structural basis for the inhibition of bacterial multidrug exporters
Ryosuke Nakashima,
Keisuke Sakurai,
Seiji Yamasaki,
Katsuhiko Hayashi,
Chikahiro Nagata,
Kazuki Hoshino,
Yoshikuni Onodera,
Kunihiko Nishino and
Akihito Yamaguchi ()
Additional contact information
Ryosuke Nakashima: Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan
Keisuke Sakurai: Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan
Seiji Yamasaki: Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka 565-0871, Japan
Katsuhiko Hayashi: Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka 565-0871, Japan
Chikahiro Nagata: Daiichi Sankyo Co. Ltd, 16-13, Kita-Kasai 1-Chome, Edogawa-ku, Tokyo 134-8630, Japan
Kazuki Hoshino: Daiichi Sankyo Co. Ltd, 16-13, Kita-Kasai 1-Chome, Edogawa-ku, Tokyo 134-8630, Japan
Yoshikuni Onodera: Daiichi Sankyo Co. Ltd, 16-13, Kita-Kasai 1-Chome, Edogawa-ku, Tokyo 134-8630, Japan
Kunihiko Nishino: Laboratory of Microbiology and Infectious Diseases, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan
Akihito Yamaguchi: Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan
Nature, 2013, vol. 500, issue 7460, 102-106
Abstract:
The first inhibitor-bound X-ray crystal structures of the bacterial multidrug efflux transporter AcrB and its homologue MexB are presented, with the inhibitor shown to bind the transporter through a narrow hydrophobic pit, thereby preventing rotation of AcrB and MexB monomers.
Date: 2013
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DOI: 10.1038/nature12300
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