5WS4

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

Summary for 5WS4

• Entry DOI: 10.2210/pdb5ws4/pdb
• Descriptor: Macrolide export ATP-binding/permease protein MacB, 5'-O-[(R)-HYDROXY(THIOPHOSPHONOOXY)PHOSPHORYL]ADENOSINE (2 entities in total)
• Functional Keywords: multi-drug efflux transporter, abc transporter, drug exporter, membrane protein
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 2
• Total formula weight: 145431.25

Authors

Murakami, S.,Okada, U.,Yamashita, E. (deposition date: 2016-12-05, release date: 2017-11-15, Last modification date: 2024-03-20)

Primary citation

Okada, U.,Yamashita, E.,Neuberger, A.,Morimoto, M.,van Veen, H.W.,Murakami, S.
Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii.
Nat Commun, 8:1336-1336, 2017

PubMed 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.

PubMed: 29109439
DOI: 10.1038/s41467-017-01399-2

Experimental method

X-RAY DIFFRACTION (3.4 Å)