The alternating access transport mechanism in LacY.
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ABSTRACT:
SUBMITTER: Kaback HR
PROVIDER: S-EPMC3030946 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature
Publications
The alternating access transport mechanism in LacY.
Kaback H Ronald HR Smirnova Irina I Kasho Vladimir V Nie Yiling Y Zhou Yonggang Y
The Journal of membrane biology 20101216 1-2
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 appr ...[more]
Similar Datasets
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