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Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket

Author

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  • Ryosuke Nakashima

    (Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka567-0047, Japan)

  • Keisuke Sakurai

    (Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka567-0047, Japan)

  • Seiji Yamasaki

    (Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka 565-0871, Japan)

  • Kunihiko Nishino

    (Laboratory of Microbiology and Infectious Diseases, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka567-0047, Japan)

  • Akihito Yamaguchi

    (Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka567-0047, Japan
    Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka 565-0871, Japan)

Abstract

Crystallographic studies show that high-molecular-mass drugs bind to the bacterial multidrug transporter AcrB at a previously unseen ‘proximal’ binding pocket before peristaltic transfer to the known ‘distal’ pocket, whereas low-molecular-mass drugs bind directly to the distal pocket.

Suggested Citation

  • Ryosuke Nakashima & Keisuke Sakurai & Seiji Yamasaki & Kunihiko Nishino & Akihito Yamaguchi, 2011. "Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket," Nature, Nature, vol. 480(7378), pages 565-569, December.
    • Handle: RePEc:nat:nature:v:480:y:2011:i:7378:d:10.1038_nature10641
    DOI: 10.1038/nature10641
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    Cited by:

    1. Alina Ornik-Cha & Julia Wilhelm & Jessica Kobylka & Hanno Sjuts & Attilio V. Vargiu & Giuliano Malloci & Julian Reitz & Anja Seybert & Achilleas S. Frangakis & Klaas M. Pos, 2021. "Structural and functional analysis of the promiscuous AcrB and AdeB efflux pumps suggests different drug binding mechanisms," Nature Communications, Nature, vol. 12(1), pages 1-14, December.

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