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The Alternating Access Transport Mechanism in LacY

  • Author(s): Kaback, H. Ronald;
  • Smirnova, Irina;
  • Kasho, Vladimir;
  • Nie, Yiling;
  • Zhou, Yonggang
  • et al.
Abstract

Lactose permease of Escherichia coli (LacY) is highly dynamic, and sugar binding causes closing of a large inward-facing cavity with opening of a wide outward-facing hydrophilic cavity. Therefore, lactose/H+ symport via LacY very likely involves a global conformational change that allows alternating access of single sugar- and H+-binding sites to either side of the membrane. Here, in honor of Stephan H. White’s seventieth birthday, we review in camera the various biochemical/biophysical approaches that provide experimental evidence for the alternating access mechanism.

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