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

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.

SUBMITTER: Okada U

PROVIDER: S-EPMC5673888 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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

Okada Ui U Yamashita Eiki E Neuberger Arthur A Morimoto Mayu M van Veen Hendrik W HW Murakami Satoshi S

Nature communications 20171106 1

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 domai ...[more]

PMID: 29109439

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