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J Membr Biol. 2011 Jan;239(1-2):85-93. doi: 10.1007/s00232-010-9327-5. Epub 2010 Dec 16.

The alternating access transport mechanism in LacY.

Author information

1
Department of Physiology, University of California Los Angeles, Los Angeles, CA 90095, USA. rkaback@mednet.ucla.edu

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.

PMID:
21161516
PMCID:
PMC3030946
DOI:
10.1007/s00232-010-9327-5
[Indexed for MEDLINE]
Free PMC Article

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