5GKO

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

5GKO の概要

• エントリーDOI: 10.2210/pdb5gko/pdb
• 分子名称: Macrolide export ATP-binding/permease protein MacB (1 entity in total)
• 機能のキーワード: multi-drug, efflux transporter, abc transporter, drug exporter, membrane protein
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 146608.12

構造登録者

Murakami, S.,Okada, U.,Yamashita, E. (登録日: 2016-07-04, 公開日: 2017-11-15, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.393 Å)