1fx8
From Proteopedia
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CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) WITH SUBSTRATE GLYCEROL
Overview
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.
About this Structure
1FX8 is a Single protein structure of sequence from Escherichia coli with BOG and GOL as ligands. Full crystallographic information is available from OCA.
Reference
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
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