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 alternati...

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Detalles Bibliográficos
Autores principales: Kaback, H. Ronald, Smirnova, Irina, Kasho, Vladimir, Nie, Yiling, Zhou, Yonggang
Formato: Texto
Lenguaje:English
Publicado: Springer-Verlag 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3030946/
https://www.ncbi.nlm.nih.gov/pubmed/21161516
http://dx.doi.org/10.1007/s00232-010-9327-5
Descripción
Sumario: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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