Ontology highlight
ABSTRACT:
SUBMITTER: Nie Y
PROVIDER: S-EPMC2906848 | biostudies-literature | 2010 May
REPOSITORIES: biostudies-literature
Nie Yiling Y Kaback H Ronald HR
Proceedings of the National Academy of Sciences of the United States of America 20100510 21
Many independent lines of evidence indicate that the lactose permease of Escherichia coli (LacY) is highly dynamic and that sugar binding causes closing of a large inward-facing cavity with opening of a wide outward-facing hydrophilic cavity. Therefore, lactose/H(+) symport catalyzed by 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 (the alternating access model). The x-ray crystal str ...[more]