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Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii

Author

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  • Ui Okada

    (Tokyo Institute of Technology)

  • Eiki Yamashita

    (Institute for Protein Research, Osaka University)

  • Arthur Neuberger

    (University of Cambridge)

  • Mayu Morimoto

    (Tokyo Institute of Technology)

  • Hendrik W. van Veen

    (University of Cambridge)

  • Satoshi Murakami

    (Tokyo Institute of Technology)

Abstract

The MacA–MacB–TolC tripartite complex is a transmembrane machine that spans both plasma membrane and outer membrane and actively extrudes substrates, including macrolide antibiotics, virulence factors, peptides and cell envelope precursors. These transport activities are driven by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. Here, we present the crystal structure of MacB at 3.4-Å resolution. MacB forms a dimer in which each protomer contains a nucleotide-binding domain and four transmembrane helices that protrude in the periplasm into a binding domain for interaction with the membrane fusion protein MacA. MacB represents an ABC transporter in pathogenic microorganisms with unique structural features.

Suggested Citation

  • Ui Okada & Eiki Yamashita & Arthur Neuberger & Mayu Morimoto & Hendrik W. van Veen & Satoshi Murakami, 2017. "Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii," Nature Communications, Nature, vol. 8(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01399-2
    DOI: 10.1038/s41467-017-01399-2
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