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

@inproceedings{Okada2017CrystalSO,
  title={Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii},
  author={Ui Okada and Eiki Yamashita and Arthur Neuberger and Mayu Morimoto and Hendrik W van Veen and Satoshi Murakami},
  booktitle={Nature Communications},
  year={2017}
}
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… CONTINUE READING
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