2J8S

Drug Export Pathway of Multidrug Exporter AcrB Revealed by DARPin Inhibitors

2J8S の概要

• エントリーDOI: 10.2210/pdb2j8s/pdb
• 関連するPDBエントリー: 1IWG 1OY6 1OY8 1OY9 1OYD 1OYE 1T9T 1T9U 1T9V 1T9W 1T9X 1T9Y 2GIF 2HRT
• 分子名称: ACRIFLAVINE RESISTANCE PROTEIN B, DARPIN, DODECYL-BETA-D-MALTOSIDE, ... (5 entities in total)
• 機能のキーワード: membrane protein-complex, designed ankyrin repeat protein, multidrug resistance protein, co-crystallization, antibiotic resistance, inner membrane, protein complex, membrane protein, rnd, membrane, inhibitor, transport, transmembrane, drug-efflux pump, transport protein, antibiotic resistance-inhibitor complex
• 由来する生物種: ESCHERICHIA COLI; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 385733.97

構造登録者

Sennhauser, G.,Amstutz, P.,Briand, C.,Storchenegger, O.,Gruetter, M.G. (登録日: 2006-10-27, 公開日: 2007-01-23, 最終更新日: 2023-12-13)

主引用文献

Sennhauser, G.,Amstutz, P.,Briand, C.,Storchenegger, O.,Grutter, M.G.
Drug Export Pathway of Multidrug Exporter Acrb Revealed by Darpin Inhibitors.
Plos Biol., 5:E7-, 2007

PubMed Abstract: The multidrug exporter AcrB is the inner membrane component of the AcrAB-TolC drug efflux system in Escherichia coli and is responsible for the resistance of this organism to a wide range of drugs. Here we describe the crystal structure of the trimeric AcrB in complex with a designed ankyrin-repeat protein (DARPin) inhibitor at 2.5-A resolution. The three subunits of AcrB are locked in different conformations revealing distinct channels in each subunit. There seems to be remote conformational coupling between the channel access, exit, and the putative proton-translocation site, explaining how the proton motive force is used for drug export. Thus our structure suggests a transport pathway not through the central pore but through the identified channels in the individual subunits, which greatly advances our understanding of the multidrug export mechanism.

PubMed: 17194213
DOI: 10.1371/JOURNAL.PBIO.0050007

実験手法

X-RAY DIFFRACTION (2.54 Å)