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Energetics of ligandinduced conformational flexibility in the lactose permease of Escherichia coli
- Publisher
- Springer Journals
- Copyright
- Copyright © 2010 by The Author(s)
- Subject
- Life Sciences; Human Physiology ; Biochemistry, general
- ISSN
- 0022-2631
- eISSN
- 1432-1424
- DOI
- 10.1007/s00232-010-9327-5
- pmid
- 21161516
- Publisher site
- See Article on Publisher Site
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.
Journal
The Journal of Membrane Biology – Springer Journals
Published: Dec 16, 2010