PMID:15313233
| Citation |
Lemieux, MJ, Huang, Y and Wang, DN (2004) The structural basis of substrate translocation by the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily. Curr. Opin. Struct. Biol. 14:405-12 |
|---|---|
| Abstract |
The major facilitator superfamily represents the largest group of secondary active membrane transporters in the cell. The 3.3A resolution structure of a member of this protein superfamily, the glycerol-3-phosphate transporter from the Escherichia coli inner membrane, reveals two domains connected by a long central loop. These N- and C-terminal domains, each containing a six-helix bundle, are related by pseudo-twofold symmetry. A substrate translocation pore is located between the two domains and is open to the cytoplasm. Two arginines at the closed end of the pore comprise the substrate-binding site. Biochemical experiments show that, upon substrate binding, the protein adopts a more compact conformation. The crystal structure suggests that the transporter operates through a single binding site, alternating access mechanism via a rocker-switch type of movement of the N- and C-terminal domains. The structure and mechanism of the glycerol-3-phosphate transporter form a paradigm for other members of the major facilitator superfamily. |
| Links |
PubMed Online version:10.1016/j.sbi.2004.06.003 |
| Keywords |
Binding Sites; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/metabolism; Models, Molecular; Monosaccharide Transport Proteins/metabolism; Protein Structure, Tertiary; Protein Transport/physiology; Structure-Activity Relationship |
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