1pw4 | pdb_00001pw4

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

spinqualitylabelsall models 1pw4, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pw4 is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: glpT ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GLPT_ECOLI] Responsible for glycerol-3-phosphate uptake. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli.,Huang Y, Lemieux MJ, Song J, Auer M, Wang DN Science. 2003 Aug 1;301(5633):616-20. PMID:12893936 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Major Facilitators

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