Covalently linked AcrB giant offers a new powerful tool for mechanistic analysis of multidrug efflux in bacteria.
Zgurskaya
Helen I
HI
University of Oklahoma, Department of Chemistry and Biochemistry, 620 Parrington Oval, Room 208, Norman, Oklahoma 73019, USA. elenaz@ou.edu
D000900:Anti-Bacterial Agents / Q000378:metabolism* / Q000494:pharmacology; D001692:Biological Transport; D003001:Cloning, Molecular; D024901:Drug Resistance, Multiple, Bacterial; D004926:Escherichia coli / Q000737:chemistry / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D027425:ATP-Binding Cassette, Sub-Family C Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D000900:Anti-Bacterial Agents; D029968:Escherichia coli Proteins; D027425:ATP-Binding Cassette, Sub-Family C Proteins; D011993:Recombinant Fusion Proteins; C083496:AcrB protein, E coli