LESSONS FROM LACTOSE PERMEASE

Annual Reviews - Tập 35 Số 1 - Trang 67-91 - 2006
Lan Guan1, H. Ronald Kaback1
1Departments of Physiology, and 2Microbiology, Immunology & Molecular Genetics, 3Molecular Biology Institute, University of California, Los Angeles, California 90095-1662;

Tóm tắt

An X-ray structure of the lactose permease of Escherichia coli (LacY) in an inward-facing conformation has been solved. LacY contains N- and C-terminal domains, each with six transmembrane helices, positioned pseudosymmetrically. Ligand is bound at the apex of a hydrophilic cavity in the approximate middle of the molecule. Residues involved in substrate binding and H+ translocation are aligned parallel to the membrane at the same level and may be exposed to a water-filled cavity in both the inward- and outward-facing conformations, thereby allowing both sugar and H+ release directly into either cavity. These structural features may explain why LacY catalyzes galactoside/H+ symport in both directions utilizing the same residues. A working model for the mechanism is presented that involves alternating access of both the sugar- and H+-binding sites to either side of the membrane.

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Annual Reviews

Tập 35 Số 1

67-91

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