2dr6 | pdb_00002dr6

Crystal structure of a multidrug transporter reveal a functionally rotating mechanism

spinqualitylabelsall models 2dr6, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2dr6 is a 3 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DM2 Related: 2dhh, 2drd Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism.,Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A Nature. 2006 Sep 14;443(7108):173-9. Epub 2006 Aug 16. PMID:16915237 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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