title: No single irreplaceable acidic residues in the Escherichia coli secondary multidrug transporter MdfA.
abstract: The largest family of solute transporters (major facilitator superfamily [MFS]) includes proton-motive-force-driven secondary transporters. Several characterized MFS transporters utilize essential acidic residues that play a critical role in the energy-coupling mechanism during transport. Surprisingly, we show here that no single acidic residue plays an irreplaceable role in the Escherichia coli secondary multidrug transporter MdfA.
authors.affiliation: Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Nadejda
authors.initials: N
authors.lastname: Sigal
authors.forename: Shahar
authors.initials: S
authors.lastname: Molshanski-Mor
authors.forename: Eitan
authors.initials: E
authors.lastname: Bibi
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000235:genetics; D001692:Biological Transport; D002701:Chloramphenicol / Q000378:metabolism; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000737:chemistry* / Q000254:growth & development / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D004996:Ethidium / Q000378:metabolism; D005470:Fluorometry; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D008956:Models, Chemical; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D013329:Structure-Activity Relationship
chemical_list: D000596:Amino Acids; D029968:Escherichia coli Proteins; C118438:Mdfa protein, E coli; D026901:Membrane Transport Proteins; D002701:Chloramphenicol; D004996:Ethidium