Exploring the role of a unique carboxyl residue in EmrE by mass spectrometry.

@article{Weinglass2005ExploringTR,
  title={Exploring the role of a unique carboxyl residue in EmrE by mass spectrometry.},
  author={Adam B. Weinglass and Misha Soskine and Jose-Luis Vazquez-Ibar and Julian P Whitelegge and Kym F. Faull and H Ronald Kaback and Shimon Schuldiner},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 9},
  pages={7487-92}
}
EmrE is a small multidrug transporter in Escherichia coli that extrudes various positively charged drugs across the plasma membrane in exchange with protons, thereby rendering cells resistant to these compounds. Biochemical experiments indicate that the basic functional unit of EmrE is a dimer where the common binding site for protons and substrate is formed by the interaction of an essential charged residue (Glu-14) from both EmrE monomers. Carbodiimide modification of EmrE has been studied… CONTINUE READING
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