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Crystal structures of a multidrug transporter reveal a functionally rotating mechanism

Author

Listed:
  • Satoshi Murakami

    (Institute of Scientific and Industrial Research, Osaka University
    PRESTO
    CREST, Japan Science and Technology Agency
    Faculty of Pharmaceutical Science)

  • Ryosuke Nakashima

    (Institute of Scientific and Industrial Research, Osaka University)

  • Eiki Yamashita

    (Institute for Protein Research, Osaka University)

  • Takashi Matsumoto

    (Institute of Scientific and Industrial Research, Osaka University
    CREST, Japan Science and Technology Agency)

  • Akihito Yamaguchi

    (Institute of Scientific and Industrial Research, Osaka University
    CREST, Japan Science and Technology Agency
    Faculty of Pharmaceutical Science)

Abstract

AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB–drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change.

Suggested Citation

  • Satoshi Murakami & Ryosuke Nakashima & Eiki Yamashita & Takashi Matsumoto & Akihito Yamaguchi, 2006. "Crystal structures of a multidrug transporter reveal a functionally rotating mechanism," Nature, Nature, vol. 443(7108), pages 173-179, September.
    • Handle: RePEc:nat:nature:v:443:y:2006:i:7108:d:10.1038_nature05076
    DOI: 10.1038/nature05076
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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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