1fx8 | pdb_00001fx8

CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) WITH SUBSTRATE GLYCEROL

spinqualitylabelsall models 1fx8, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fx8 is a 1 chain structure. The May 2014 RCSB PDB Molecule of the Month feature on Aquaporin by David Goodsell is 10.2210/rcsb_pdb/mom_2014_5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BOG, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GLPF_ECOLI] Transporter of glycerol across the cytoplasmic membrane, with limited permeability to water and small uncharged compounds such as polyols. 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 Membrane channel proteins of the aquaporin family are highly selective for permeation of specific small molecules, with absolute exclusion of ions and charged solutes and without dissipation of the electrochemical potential across the cell membrane. We report the crystal structure of the Escherichia coli glycerol facilitator (GlpF) with its primary permeant substrate glycerol at 2.2 angstrom resolution. Glycerol molecules line up in an amphipathic channel in single file. In the narrow selectivity filter of the channel the glycerol alkyl backbone is wedged against a hydrophobic corner, and successive hydroxyl groups form hydrogen bonds with a pair of acceptor, and donor atoms. Two conserved aspartic acid-proline-alanine motifs form a key interface between two gene-duplicated segments that each encode three-and-one-half membrane-spanning helices around the channel. This structure elucidates the mechanism of selective permeability for linear carbohydrates and suggests how ions and water are excluded. Structure of a glycerol-conducting channel and the basis for its selectivity.,Fu D, Libson A, Miercke LJ, Weitzman C, Nollert P, Krucinski J, Stroud RM Science. 2000 Oct 20;290(5491):481-6. PMID:11039922 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aquaporin Ion channels

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