Specificity of the glucose channel formed by protein D1 of Pseudomonas aeruginosa.
Protein D1 from the outer membrane of Pseudomonas aeruginosa was purified and reconstituted into proteoliposomes. Many small molecules were shown to diffuse through the D1 channel in the proteoliposomes, and the permeation rates of D-glucose, L-glucose, D-xylose, and L-xylose were much higher than expected for their size. This finding and the permeation rates of various glucose analogs suggest that, although the channel has a specific recognition site for glucose, it functions in a manner very different from that of the glucose carrier of erythrocytes.
D001425:Bacterial Outer Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002462:Cell Membrane / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D004058:Diffusion; D005947:Glucose / Q000031:analogs & derivatives / Q000378:metabolism*; D007473:Ion Channels / Q000378:metabolism*; D008081:Liposomes / Q000378:metabolism*; D008970:Molecular Weight; D018272:Porins; D011550:Pseudomonas aeruginosa / Q000032:analysis*; D013329:Structure-Activity Relationship; D014994:Xylose / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D007473:Ion Channels; D008081:Liposomes; D018272:Porins; D014994:Xylose; D005947:Glucose