Structural basis of human erythrocyte glucose transporter function in reconstituted vesicles.
The transmembrane orientation of the human erythrocyte glucose transporter was assessed based on polarized Fourier transform infrared and ultraviolet circular dichroism spectroscopic data obtained from oriented multilamellar films of the reconstituted transporter vesicles. Infrared spectra revealed that there are distinct vibrations for alpha-helical structure while the vibrational frequencies specific to beta-structure are characteristically absent. Analysis of linear dichroism of the infrared spectra further indicated that these alpha-helices in the transporter are preferentially oriented perpendicular to the lipid bilayer plane forming an effective tilt of less than 38 degrees from the membrane normal. Such a preferential orientation was further supported by ultraviolet circular dichroism spectra which reveal that the 208 nm Moffit band found in the detergent-solubilized preparation is absent in the film preparation. Linear dichroism data further indicated that D-glucose, a typical substrate, further reduces this effective tilt angle slightly.
Chin
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Jung
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Jung
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D002850:Chromatography, Gel; D002942:Circular Dichroism; D004912:Erythrocytes / Q000032:analysis*; D006801:Humans; D009004:Monosaccharide Transport Proteins / Q000502:physiology; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
D009004:Monosaccharide Transport Proteins