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Structural Basis of the Multiple Binding Capacity of the AcrB Multidrug Efflux PumpStructural Basis of the Multiple Binding Capacity of the AcrB Multidrug Efflux Pump
Structural highlights
Function[ACRB_ECOLI] AcrAB is a drug efflux protein with a broad substrate specificity.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMultidrug 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. Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump.,Yu EW, McDermott G, Zgurskaya HI, Nikaido H, Koshland DE Jr Science. 2003 May 9;300(5621):976-80. PMID:12738864[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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