1OY8

Structural Basis of Multiple Drug Binding Capacity of the AcrB Multidrug Efflux Pump

Summary for 1OY8

• Entry DOI: 10.2210/pdb1oy8/pdb
• Descriptor: Acriflavine resistance protein B, RHODAMINE 6G (2 entities in total)
• Functional Keywords: membrane protein
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P31224
• Total number of polymer chains: 1
• Total formula weight: 114108.74

Authors

Yu, E.W.,McDermott, G.,Zgurskaya, H.I.,Nikaido, H.,Koshland Jr., D.E. (deposition date: 2003-04-03, release date: 2003-05-13, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.63 Å)