The alternating access transport mechanism in LacY.

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.

SUBMITTER: Kaback HR 

PROVIDER: S-EPMC3030946 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature