Structural comparison of lactose permease and the glycerol-3-phosphate antiporter: members of the major facilitator superfamily.
Structural knowledge of the major facilitator superfamily has dramatically increased during the past year with the emergence of the structures of three members of this family of transporters. All three structures reveal 12 transmembrane helices forming two distinct domains, and could imply that members of this superfamily have preserved both secondary and tertiary structure elements during evolution.
Abramson
Jeff
J
Department of Biological Sciences, Imperial College London, London SW7 2AZ, UK.
Kaback
H Ronald
HR
Iwata
So
S
D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009004:Monosaccharide Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D021381:Protein Transport / Q000502:physiology; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D027981:Symporters / Q000737:chemistry* / Q000378:metabolism
D029968:Escherichia coli Proteins; C488962:GlpT protein, E coli; C050221:LacY protein, E coli; D026901:Membrane Transport Proteins; D009004:Monosaccharide Transport Proteins; D027981:Symporters