Conformational changes in a bacterial multidrug transporter are phosphatidylethanolamine-dependent

@article{Gbaguidi2007ConformationalCI,
  title={Conformational changes in a bacterial multidrug transporter are phosphatidylethanolamine-dependent},
  author={B{\'e}n{\'e}dicte Gbaguidi and Pierre Hakizimana and Guy Vandenbussche and Jean Marie Ruysschaert},
  journal={Cellular and Molecular Life Sciences},
  year={2007},
  volume={64},
  pages={1571-1582}
}
Abstract.LmrP is an electrogenic H+/drug antiporter that extrudes a broad spectrum of antibiotics. Five carboxylic residues are implicated in drug binding (Asp142 and Glu327) and proton motive force-mediated restructuring (Asp68, Asp128 and Asp235). ATR-FTIR (Attenuated Total Reflection — Fourier Transform Infrared) and tryptophan quenching experiments revealed that phosphatidylethanolamine (PE) is required to generate the structural intermediates induced by ionization of carboxylic residues… 
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