7B8Q

Acinetobacter baumannii multidrug transporter AdeB in L*OO state

7B8Q の概要

• エントリーDOI: 10.2210/pdb7b8q/pdb
• EMDBエントリー: 12089
• 分子名称: Efflux pump membrane transporter (1 entity in total)
• 機能のキーワード: rnd-transporter, multidrug transporter, antibiotic resistance, membrane protein, transport protein
• 由来する生物種: Acinetobacter baumannii (strain AYE)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 345429.16

構造登録者

Ornik-Cha, A.,Reitz, J.,Seybert, A.,Frangakis, A.,Pos, K.M. (登録日: 2020-12-13, 公開日: 2021-10-20, 最終更新日: 2024-07-10)

主引用文献

Ornik-Cha, A.,Wilhelm, J.,Kobylka, J.,Sjuts, H.,Vargiu, A.V.,Malloci, G.,Reitz, J.,Seybert, A.,Frangakis, A.S.,Pos, K.M.
Structural and functional analysis of the promiscuous AcrB and AdeB efflux pumps suggests different drug binding mechanisms.
Nat Commun, 12:6919-6919, 2021

PubMed Abstract: Upon antibiotic stress Gram-negative pathogens deploy resistance-nodulation-cell division-type tripartite efflux pumps. These include a H/drug antiporter module that recognizes structurally diverse substances, including antibiotics. Here, we show the 3.5 Å structure of subunit AdeB from the Acinetobacter baumannii AdeABC efflux pump solved by single-particle cryo-electron microscopy. The AdeB trimer adopts mainly a resting state with all protomers in a conformation devoid of transport channels or antibiotic binding sites. However, 10% of the protomers adopt a state where three transport channels lead to the closed substrate (deep) binding pocket. A comparison between drug binding of AdeB and Escherichia coli AcrB is made via activity analysis of 20 AdeB variants, selected on basis of side chain interactions with antibiotics observed in the AcrB periplasmic domain X-ray co-structures with fusidic acid (2.3 Å), doxycycline (2.1 Å) and levofloxacin (2.7 Å). AdeABC, compared to AcrAB-TolC, confers higher resistance to E. coli towards polyaromatic compounds and lower resistance towards antibiotic compounds.

PubMed: 34824229
DOI: 10.1038/s41467-021-27146-2

実験手法

ELECTRON MICROSCOPY (3.84 Å)