2F1V

Outer membrane protein OmpW

2F1V の概要

• エントリーDOI: 10.2210/pdb2f1v/pdb
• 関連するPDBエントリー: 2F1T
• 分子名称: Outer membrane protein W, GLYCEROL (2 entities in total)
• 機能のキーワード: outer membrane protein beta barrel, membrane protein
• 由来する生物種: Escherichia coli K12
• 細胞内の位置: Cell outer membrane: P0A915
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 130753.18

構造登録者

van den Berg, B. (登録日: 2005-11-15, 公開日: 2006-01-24, 最終更新日: 2023-08-23)

主引用文献

Hong, H.,Patel, D.R.,Tamm, L.K.,van den Berg, B.
The outer membrane protein OmpW forms an eight-stranded beta-barrel with a hydrophobic channel.
J.Biol.Chem., 281:7568-7577, 2006

PubMed Abstract: Escherichia coli OmpW belongs to a family of small outer membrane proteins that are widespread in Gram-negative bacteria. Their functions are unknown, but recent data suggest that they may be involved in the protection of bacteria against various forms of environmental stress. To gain insight into the function of these proteins A we have determined the crystal structure of E. coli OmpW to 2.7-A resolution. The structure shows that OmpW forms an 8-stranded beta-barrel with a long and narrow hydrophobic channel that contains a bound n-dodecyl-N,N-dimethylamine-N-oxide detergent molecule. Single channel conductance experiments show that OmpW functions as an ion channel in planar lipid bilayers. The channel activity can be blocked by the addition of n-dodecyl-N,N-dimethylamine-N-oxide. Taken together, the data suggest that members of the OmpW family could be involved in the transport of small hydrophobic molecules across the bacterial outer membrane.

PubMed: 16414958
DOI: 10.1074/jbc.M512365200

実験手法

X-RAY DIFFRACTION (2.7 Å)