1FX8

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

1FX8 の概要

• エントリーDOI: 10.2210/pdb1fx8/pdb
• 分子名称: GLYCEROL UPTAKE FACILITATOR PROTEIN, octyl beta-D-glucopyranoside, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: glycerol-conducting membrane channel protein, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P11244
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30953.23

構造登録者

Fu, D.,Libson, A.,Miercke, L.J.W.,Weitzman, C.,Nollert, P.,Stroud, R.M. (登録日: 2000-09-25, 公開日: 2000-11-01, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)