PMID:16675700

Citation	Yin, Y, He, X, Szewczyk, P, Nguyen, T and Chang, G (2006) Structure of the multidrug transporter EmrD from Escherichia coli. Science 312:741-4
Abstract	EmrD is a multidrug transporter from the Major Facilitator Superfamily that expels amphipathic compounds across the inner membrane of Escherichia coli. Here, we report the x-ray structure of EmrD determined to a resolution of 3.5 angstroms. The structure reveals an interior that is composed mostly of hydrophobic residues, which is consistent with its role transporting amphipathic molecules. Two long loops extend into the inner leaflet side of the cell membrane. This region can serve to recognize and bind substrate directly from the lipid bilayer. We propose that multisubstrate specificity, binding, and transport are facilitated by these loop regions and the internal cavity.
Links	PubMed PMC3152482 Online version:10.1126/science.1125629
Keywords	Amino Acid Sequence; Biological Transport; Carbonyl Cyanide m-Chlorophenyl Hydrazone/metabolism; Cell Membrane/chemistry; Crystallography, X-Ray; Cytoplasm/chemistry; Dimerization; Drug Resistance, Multiple, Bacterial; Escherichia coli/chemistry; Escherichia coli/drug effects; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Hydrophobic and Hydrophilic Interactions; Lipid Bilayers; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Substrate Specificity
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