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      Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli.

      Science (New York, N.Y.)

      Protein Structure, Secondary, Protein Structure, Tertiary, Cell Membrane, chemistry, Crystallization, Crystallography, X-Ray, Escherichia coli, Biological Transport, enzymology, Escherichia coli Proteins, metabolism, Glycerophosphates, Helix-Turn-Helix Motifs, Mass Spectrometry, Membrane Transport Proteins, Models, Molecular, Molecular Sequence Data, Periplasm, Phosphates, Protein Conformation, Protein Folding, Amino Acid Sequence, Binding Sites

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          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.

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          Journal
          10.1126/science.1087619
          12893936

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