PMID:12893936

Citation	Huang, Y, Lemieux, MJ, Song, J, Auer, M and Wang, DN (2003) Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301:616-20
Abstract	The major facilitator superfamily represents the largest group of secondary membrane transporters in the cell. Here we report the 3.3 angstrom resolution structure of a member of this superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm. The amino- and carboxyl-terminal halves of the protein exhibit a pseudo two-fold symmetry. Closed off to the periplasm, a centrally located substrate-translocation pore contains two arginines at its closed end, which comprise the substrate-binding site. Upon substrate binding, the protein adopts a more compact conformation. We propose that GlpT operates by a single-binding site, alternating-access mechanism through a rocker-switch type of movement.
Links	PubMed Online version:10.1126/science.1087619
Keywords	Amino Acid Sequence; Binding Sites; Biological Transport; Cell Membrane/chemistry; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Glycerophosphates/metabolism; Helix-Turn-Helix Motifs; Mass Spectrometry; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Periplasm/metabolism; Phosphates/metabolism; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary
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