PMID:16946072

Citation	Seeger, MA, Schiefner, A, Eicher, T, Verrey, F, Diederichs, K and Pos, KM (2006) Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 313:1295-8
Abstract	The AcrA/AcrB/TolC complex spans the inner and outer membranes of Escherichia coli and serves as its major drug-resistance pump. Driven by the proton motive force, it mediates the efflux of bile salts, detergents, organic solvents, and many structurally unrelated antibiotics. Here, we report a crystallographic structure of trimeric AcrB determined at 2.9 and 3.0 angstrom resolution in space groups that allow asymmetry of the monomers. This structure reveals three different monomer conformations representing consecutive states in a transport cycle. The structural data imply an alternating access mechanism and a novel peristaltic mode of drug transport by this type of transporter.
Links	PubMed Online version:10.1126/science.1131542
Keywords	Biological Transport; Crystallization; Crystallography, X-Ray; Diffusion; Drug Resistance, Multiple, Bacterial; Escherichia coli/chemistry; Escherichia coli/drug effects; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/metabolism; Models, Molecular; Multidrug Resistance-Associated Proteins/chemistry; Multidrug Resistance-Associated Proteins/metabolism; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Protons
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