1IWG

Crystal structure of Bacterial Multidrug Efflux transporter AcrB

1IWG の概要

• エントリーDOI: 10.2210/pdb1iwg/pdb
• 分子名称: AcrB (1 entity in total)
• 機能のキーワード: drug resistance, multidrug efflux, transporter, antiporter, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P31224
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 114217.74

構造登録者

Murakami, S.,Nakashima, R.,Yamashita, E.,Yamaguchi, A. (登録日: 2002-05-15, 公開日: 2002-10-23, 最終更新日: 2023-12-27)

主引用文献

Murakami, S.,Nakashima, R.,Yamashita, E.,Yamaguchi, A.
Crystal structure of bacterial multidrug efflux transporter AcrB
NATURE, 419:587-593, 2002

PubMed Abstract: AcrB is a major multidrug exporter in Escherichia coli. It cooperates with a membrane fusion protein, AcrA, and an outer membrane channel, TolC. We have determined the crystal structure of AcrB at 3.5 A resolution. Three AcrB protomers are organized as a homotrimer in the shape of a jellyfish. Each protomer is composed of a transmembrane region 50 A thick and a 70 A protruding headpiece. The top of the headpiece opens like a funnel, where TolC might directly dock into AcrB. A pore formed by three alpha-helices connects the funnel with a central cavity located at the bottom of the headpiece. The cavity has three vestibules at the side of the headpiece which lead into the periplasm. In the transmembrane region, each protomer has twelve transmembrane alpha-helices. The structure implies that substrates translocated from the cell interior through the transmembrane region and from the periplasm through the vestibules are collected in the central cavity and then actively transported through the pore into the TolC tunnel.

PubMed: 12374972
DOI: 10.1038/nature01050

実験手法

X-RAY DIFFRACTION (3.5 Å)