Structure and mechanism of the lactose permease of Escherichia coli.

@article{Abramson2003StructureAM,
  title={Structure and mechanism of the lactose permease of Escherichia coli.},
  author={Jeff Abramson and Irina Smirnova and Vladimir N Kasho and Gillian E Verner and H Ronald Kaback and So Iwata},
  journal={Science},
  year={2003},
  volume={301 5633},
  pages={610-5}
}
Membrane transport proteins that transduce free energy stored in electrochemical ion gradients into a concentration gradient are a major class of membrane proteins. We report the crystal structure at 3.5 angstroms of the Escherichia coli lactose permease, an intensively studied member of the major facilitator superfamily of transporters. The molecule is composed of N- and C-terminal domains, each with six transmembrane helices, symmetrically positioned within the permease. A large internal… CONTINUE READING
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