| Автор | Guan, Lan |
| Автор | Kaback, H. Ronald |
| Дата выпуска | 2006 |
| dc.description | Abstract 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<sup>+</sup> 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<sup>+</sup> release directly into either cavity. These structural features may explain why LacY catalyzes galactoside/H<sup>+</sup> 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<sup>+</sup>-binding sites to either side of the membrane. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | LESSONS FROM LACTOSE PERMEASE |
| DOI | 10.1146/annurev.biophys.35.040405.102005 |
| Print ISSN | 1056-8700 |
| Журнал | Annual Review of Biophysics and Biomolecular Structure |
| Том | 35 |
| Первая страница | 67 |
| Последняя страница | 91 |
| Аффилиация | Guan, Lan; Departments of Physiology, and 2Microbiology, Immunology & Molecular Genetics, 3Molecular Biology Institute, University of California, Los Angeles, California 90095-1662; email: LanGuan@mednet.ucla.edu ; RKaback@mednet.ucla.edu |
