1FX8

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

Summary for 1FX8

• Entry DOI: 10.2210/pdb1fx8/pdb
• Descriptor: GLYCEROL UPTAKE FACILITATOR PROTEIN, octyl beta-D-glucopyranoside, GLYCEROL, ... (4 entities in total)
• Functional Keywords: glycerol-conducting membrane channel protein, membrane protein
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P11244
• Total number of polymer chains: 1
• Total formula weight: 30953.23

Authors

Fu, D.,Libson, A.,Miercke, L.J.W.,Weitzman, C.,Nollert, P.,Stroud, R.M. (deposition date: 2000-09-25, release date: 2000-11-01, Last modification date: 2024-02-07)

Primary citation

Fu, D.,Libson, A.,Miercke, L.J.,Weitzman, C.,Nollert, P.,Krucinski, J.,Stroud, R.M.
Structure of a glycerol-conducting channel and the basis for its selectivity.
Science, 290:481-486, 2000

PubMed Abstract: 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.

PubMed: 11039922
DOI: 10.1126/science.290.5491.481

Experimental method

X-RAY DIFFRACTION (2.2 Å)