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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The alternating access transport mechanism in LacY.

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.[1]

References

  1. The alternating access transport mechanism in LacY. Kaback, H.R., Smirnova, I., Kasho, V., Nie, Y., Zhou, Y. J. Membr. Biol. (2011) [Pubmed]
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