This entry represents the major facilitator superfamily (MFS) domain, which consists of twelve transmembrane helices. MFS proteins are the largest group of secondary membrane transporters in the cell. Among the different families of transporters, only two occur ubiquitously in all classifications of organisms; these are the ATP-Binding Cassette (ABC) superfamily and the Major Facilitator Superfamily (MFS). The MFS transporters are single-polypeptide secondary carriers capable only of transporting small solutes in response to chemiosmotic ion gradients [1, 2]. The MFS family contains members that function as uniporters, symporters or antiporters. In addition their solute specificity are also diverse. MFS proteins contain 12 transmembrane regions (with some variations).

This domain can be found in glycerol-3-phosphate transporter from Escherichia coli, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm [3]. The E. coli proton/sugar transporter lactose permease (LacY) also carries this domain, and acts to couple lactose and H+ translocation [4, 5].

1. Major facilitator superfamily. Microbiol. Mol. Biol. Rev. 62, 1-34
2. Sugar transporters from bacteria, parasites and mammals: structure-activity relationships. Trends Biochem. Sci. 23, 476-81
3. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301, 616-20
4. Structure and mechanism of the lactose permease of Escherichia coli. Science 301, 610-5
5. Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY. EMBO J. 25, 1177-83

This entry represents the major facilitator superfamily (MFS) domain, which consists of twelve tr
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