1OYD

Structural Basis of Multiple Binding Capacity of the AcrB multidrug Efflux Pump

1OYD の概要

• エントリーDOI: 10.2210/pdb1oyd/pdb
• 分子名称: Acriflavine resistance protein B, DEQUALINIUM (2 entities in total)
• 機能のキーワード: 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: 114121.84

構造登録者

Yu, E.W.,MeDermott, G.,Zgurskaya, H.I.,Nikaido, H.,Koshland Jr., D.E. (登録日: 2003-04-03, 公開日: 2003-05-13, 最終更新日: 2024-02-14)

主引用文献

Yu, E.W.,McDermott, G.,Zgurskaya, H.I.,Nikaido, H.,Koshland, D.E.
Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump.
Science, 300:976-980, 2003

PubMed Abstract: Multidrug efflux pumps cause serious problems in cancer chemotherapy and treatment of bacterial infections. Yet high-resolution structures of ligand transporter complexes have previously been unavailable. We obtained x-ray crystallographic structures of the trimeric AcrB pump from Escherichia coli with four structurally diverse ligands. The structures show that three molecules of ligands bind simultaneously to the extremely large central cavity of 5000 cubic angstroms, primarily by hydrophobic, aromatic stacking and van der Waals interactions. Each ligand uses a slightly different subset of AcrB residues for binding. The bound ligand molecules often interact with each other, stabilizing the binding.

PubMed: 12738864
DOI: 10.1126/science.1083137

実験手法

X-RAY DIFFRACTION (3.8 Å)