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Crystal structure of tripartite-type ABC transporter, MacB from Acinetobacter baumanniiCrystal structure of tripartite-type ABC transporter, MacB from Acinetobacter baumannii
Structural highlights
Function[A0A0D8G707_ACIBA] Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.[HAMAP-Rule:MF_01720] Publication Abstract from PubMedThe 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-A 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. Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii.,Okada U, Yamashita E, Neuberger A, Morimoto M, van Veen HW, Murakami S Nat Commun. 2017 Nov 6;8(1):1336. doi: 10.1038/s41467-017-01399-2. PMID:29109439[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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