Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii.
Published version
Peer-reviewed
Repository URI
Repository DOI
Change log
Authors
Okada, Ui https://orcid.org/0000-0001-7633-9308
Yamashita, Eiki
Neuberger, Arthur https://orcid.org/0000-0002-7744-6559
Morimoto, Mayu
van Veen, Hendrik W https://orcid.org/0000-0002-9658-8077
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.
Description
Keywords
ATP-Binding Cassette Transporters, Acinetobacter baumannii, Amino Acid Sequence, Bacterial Proteins, Conserved Sequence, Crystallography, X-Ray, Drug Resistance, Multiple, Bacterial, Escherichia coli, Models, Molecular, Protein Domains, Protein Structure, Quaternary, Recombinant Proteins, Sequence Homology, Amino Acid
Journal Title
Nat Commun
Conference Name
Journal ISSN
2041-1723
2041-1723
2041-1723
Volume Title
8
Publisher
Springer Science and Business Media LLC
Publisher DOI
Sponsorship
Human Frontier Science Program (HFSP) (RPG0034/2013)
Biotechnology and Biological Sciences Research Council (BB/K017713/1)
Biotechnology and Biological Sciences Research Council (BB/R00224X/1)
MRC (MC_PC_14116 v2)
Biotechnology and Biological Sciences Research Council (BB/K017713/1)
Biotechnology and Biological Sciences Research Council (BB/R00224X/1)
MRC (MC_PC_14116 v2)