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Article: Lactose Permease H+-Lactose Symporter: Mechanical Switch or Brownian Ratchet?
- Article from:
- Biophysical Journal
- Article date:
- May 15, 2007
- Author:
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Copyright informationCopyright Biophysical Society May 15, 2007. Provided by ProQuest LLC. (Hide copyright information)
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ABSTRACT
Lactose permease structure is deemed consistent with a mechanical switch device for H+-coupled symport. Because the crystallography-assigned docking position of thiodigalactoside (TDG) does not make close contact with several amino acids essential for symport; the switch model req
uires allosteric interactions between the proton and sugar binding sites. The docking program, Autodock 3 reveals other lactose-docking sites. An alternative cotransport mechanism is proposed where His-322 imidazolium, positioned in the central pore equidistant (5-7 [Angstrom]) between six charged amino acids, Arg-302 and Lys-319 opposing Glu-269, Glu-325, Asp-237, and Asp-240, transfers a proton ...
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