Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY
Research output: Contribution to journal › Journal article › Research › peer-review
Cation-coupled active transport is an essential cellular process found ubiquitously in all living organisms. Here, we present two novel ligand-free X-ray structures of the lactose permease (LacY) of Escherichia coli determined at acidic and neutral pH, and propose a model for the mechanism of coupling between lactose and H+ translocation. No sugar-binding site is observed in the absence of ligand, and deprotonation of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the initial step in H+ transduction.
Original language | English |
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Journal | E M B O Journal |
Volume | 25 |
Issue number | 6 |
Pages (from-to) | 1177-83 |
Number of pages | 7 |
ISSN | 0261-4189 |
DOIs | |
Publication status | Published - 22 Mar 2006 |
- Binding Sites, Escherichia coli, Escherichia coli Proteins, Hydrogen-Ion Concentration, Ion Transport, Lactose, Ligands, Monosaccharide Transport Proteins, Protein Conformation, Substrate Specificity, Symporters, X-Ray Diffraction
Research areas
ID: 44863912