1PW4

Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli

Summary for 1PW4

• Entry DOI: 10.2210/pdb1pw4/pdb
• Descriptor: Glycerol-3-phosphate transporter (1 entity in total)
• Functional Keywords: glycerol-3-phosphate, transmembrane, inner membrane, transporter, major facilitator superfamily, secondary active membrane transporter, membrane protein
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P08194
• Total number of polymer chains: 1
• Total formula weight: 50243.96

Authors

Huang, Y.,Lemieux, M.J.,Song, J.,Auer, M.,Wang, D.N. (deposition date: 2003-06-30, release date: 2003-08-05, Last modification date: 2024-02-14)

Primary citation

Huang, Y.,Lemieux, M.J.,Song, J.,Auer, M.,Wang, D.N.
Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia Coli
Science, 301:616-620, 2003

PubMed 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.

PubMed: 12893936
DOI: 10.1126/science.1087619

Experimental method

X-RAY DIFFRACTION (3.3 Å)