4ZIT

Crystal structure of AcrB in P21 space group

4ZIT の概要

• エントリーDOI: 10.2210/pdb4zit/pdb
• 分子名称: Multidrug efflux pump subunit AcrB, DODECYL-BETA-D-MALTOSIDE, NICKEL (II) ION (3 entities in total)
• 機能のキーワード: acrb, rnd efflux pump, bacterial multidrug resistance, export mechanism, transport protein
• 由来する生物種: Escherichia coli K-12
• 細胞内の位置: Cell inner membrane ; Multi- pass membrane protein : P31224
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 685230.85

構造登録者

Ababou, A.,Koronakis, V. (登録日: 2015-04-28, 公開日: 2016-07-27, 最終更新日: 2024-01-10)

主引用文献

Ababou, A.,Koronakis, V.
Structures of Gate Loop Variants of the AcrB Drug Efflux Pump Bound by Erythromycin Substrate.
Plos One, 11:e0159154-e0159154, 2016

PubMed Abstract: Gram-negative bacteria such as E. coli use tripartite efflux pumps such as AcrAB-TolC to expel antibiotics and noxious compounds. A key feature of the inner membrane transporter component, AcrB, is a short stretch of residues known as the gate/switch loop that divides the proximal and distal substrate binding pockets. Amino acid substitutions of the gate loop are known to decrease antibiotic resistance conferred by AcrB. Here we present two new AcrB gate loop variants, the first stripped of its bulky side chains, and a second in which the gate loop is removed entirely. By determining the crystal structures of the variant AcrB proteins in the presence and absence of erythromycin and assessing their ability to confer erythromycin tolerance, we demonstrate that the gate loop is important for AcrB export activity but is not required for erythromycin binding.

PubMed: 27403665
DOI: 10.1371/journal.pone.0159154

実験手法

X-RAY DIFFRACTION (3.296 Å)