2DHH

Crystal structure of a multidrug transporter reveal a functionally rotating mechanism

2DHH の概要

• エントリーDOI: 10.2210/pdb2dhh/pdb
• 関連するPDBエントリー: 2DR6 2DRD
• 分子名称: ACRB (2 entities in total)
• 機能のキーワード: membrane transporter, membrane protein, multidrug efflux, drug resistance, transporter, exporter, antiporter
• 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: 3
• 化学式量合計: 342653.23

構造登録者

Murakami, S.,Nakashima, R.,Yamashita, E.,Matsumoto, T. (登録日: 2006-03-23, 公開日: 2006-08-22, 最終更新日: 2024-03-13)

主引用文献

Murakami, S.,Nakashima, R.,Yamashita, E.,Matsumoto, T.,Yamaguchi, A.
Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
Nature, 443:173-179, 2006

PubMed Abstract: AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change.

PubMed: 16915237
DOI: 10.1038/nature05076

実験手法

X-RAY DIFFRACTION (2.8 Å)