5V5S

multi-drug efflux; membrane transport; RND superfamily; Drug resistance

5V5S の概要

• エントリーDOI: 10.2210/pdb5v5s/pdb
• EMDBエントリー: 8636
• 分子名称: Outer membrane protein TolC, Multidrug efflux pump subunit AcrA, Multidrug efflux pump subunit AcrB (3 entities in total)
• 機能のキーワード: multi-drug efflux, membrane transport, rnd superfamily, drug resistance, membrane protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 740586.44

構造登録者

wang, Z.,fan, G.,Hryc, C.F.,Blaza, J.N.,Serysheva, I.I.,Schmid, M.F.,Chiu, W.,Luisi, B.F.,Du, D. (登録日: 2017-03-15, 公開日: 2017-04-19, 最終更新日: 2024-11-20)

主引用文献

Wang, Z.,Fan, G.,Hryc, C.F.,Blaza, J.N.,Serysheva, I.I.,Schmid, M.F.,Chiu, W.,Luisi, B.F.,Du, D.
An allosteric transport mechanism for the AcrAB-TolC Multidrug Efflux Pump.
Elife, 6:-, 2017

PubMed Abstract: Bacterial efflux pumps confer multidrug resistance by transporting diverse antibiotics from the cell. In Gram-negative bacteria, some of these pumps form multi-protein assemblies that span the cell envelope. Here, we report the near-atomic resolution cryoEM structures of the AcrAB-TolC multidrug efflux pump in resting and drug transport states, revealing a quaternary structural switch that allosterically couples and synchronizes initial ligand binding with channel opening. Within the transport-activated state, the channel remains open even though the pump cycles through three distinct conformations. Collectively, our data provide a dynamic mechanism for the assembly and operation of the AcrAB-TolC pump.

PubMed: 28355133
DOI: 10.7554/eLife.24905

実験手法

ELECTRON MICROSCOPY (6.5 Å)