The structure of the lactose permease derived from Raman spectroscopy and prediction methods.
The secondary structure of the lactose permease of Escherichia coli reconstituted in lipid membranes was determined by Raman spectroscopy. The alpha-helix content is approximately 70%, the beta-strand content below 10% and beta-turns contribute 15%. About 1/3 of the residues in alpha-helices and most other residues are exposed to water. Employing a method for structural prediction which accounts for amphipathic helices, 10 membrane-spanning helices are predicted which are either hydrophobic or amphipathic. They are expected to form an outer ring of helices in the membrane. The interior of the ring would be made of residues which are predominantly hydrophilic and, evoking the analogy to sugar-binding proteins, suited to provide the sugar binding site.
D004926:Escherichia coli; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D008962:Models, Theoretical; D009004:Monosaccharide Transport Proteins; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman; D027981:Symporters
D029968:Escherichia coli Proteins; C050221:LacY protein, E coli; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D009004:Monosaccharide Transport Proteins; D027981:Symporters; C021499:lactose permease