5JMN

Fusidic acid bound AcrB

5JMN の概要

• エントリーDOI: 10.2210/pdb5jmn/pdb
• 分子名称: Multidrug efflux pump subunit AcrB, DODECANE, N-OCTANE, ... (14 entities in total)
• 機能のキーワード: multidrug efflux protein, membrane protein, transport protein
• 由来する生物種: Escherichia coli (strain K12); 詳細
• 細胞内の位置: Cell inner membrane ; Multi- pass membrane protein : P31224
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 393607.11

構造登録者

Oswald, C.,Tam, H.K.,Pos, K.M. (登録日: 2016-04-29, 公開日: 2016-12-21, 最終更新日: 2024-01-10)

主引用文献

Oswald, C.,Tam, H.K.,Pos, K.M.
Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB.
Nat Commun, 7:13819-13819, 2016

PubMed Abstract: The deployment of multidrug efflux pumps is a powerful defence mechanism for Gram-negative bacterial cells when exposed to antimicrobial agents. The major multidrug efflux transport system in Escherichia coli, AcrAB-TolC, is a tripartite system using the proton-motive force as an energy source. The polyspecific substrate-binding module AcrB uses various pathways to sequester drugs from the periplasm and outer leaflet of the inner membrane. Here we report the asymmetric AcrB structure in complex with fusidic acid at a resolution of 2.5 Å and mutational analysis of the putative fusidic acid binding site at the transmembrane domain. A groove shaped by the interface between transmembrane helix 1 (TM1) and TM2 specifically binds fusidic acid and other lipophilic carboxylated drugs. We propose that these bound drugs are actively displaced by an upward movement of TM2 towards the AcrB periplasmic porter domain in response to protonation events in the transmembrane domain.

PubMed: 27982032
DOI: 10.1038/ncomms13819

実験手法

X-RAY DIFFRACTION (2.5 Å)