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

Ui Okada, Eiki Yamashita, Arthur Neuberger, Mayu Morimoto, Hendrik W. van Veen and Satoshi Murakami ()
Additional contact information
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

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: 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.

Date: 2017
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-017-01399-2 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01399-2

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-017-01399-2

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().