2j8s

DRUG EXPORT PATHWAY OF MULTIDRUG EXPORTER ACRB REVEALED BY DARPIN INHIBITORS

spinqualitylabelsall models 2j8s, resolution 2.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2j8s is a 5 chain structure with sequence from [1] and Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: LMT, LMU Related: 1iwg, 1oy6, 1oy8, 1oy9, 1oyd, 1oye, 1t9t, 1t9u, 1t9v, 1t9w, 1t9x, 1t9y, 2gif, 2hrt Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [ACRB_ECOLI] AcrAB is a drug efflux protein with a broad substrate specificity. 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 PubMed 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. Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors.,Sennhauser G, Amstutz P, Briand C, Storchenegger O, Grutter MG PLoS Biol. 2007 Jan;5(1):e7. PMID:17194213 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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