The outer membrane protein OmpW forms an eight-stranded β-barrel with a hydrophobic channel
The outer membrane protein OmpW forms an eight-stranded β-barrel with a hydrophobic channel
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DOI：
10.1074/jbc.m512365200
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发表时间：
2006-03-17
影响因子：
4.8
通讯作者：
van den Berg, B
中科院分区：
文献类型：
--
作者：
Hong, HD;Patel, DR;van den Berg, B
大肠杆菌OmpW属于广泛存在于革兰氏阴性菌中的小外膜蛋白家族。它们的功能尚不清楚，但最近的数据表明，它们可能参与保护细菌免受各种形式的环境压力。为了深入了解这些蛋白质的功能，我们确定了大肠杆菌OmpW的晶体结构，分辨率为2.7埃。结构表明，OmpW形成一个8链β -桶状结构，具有长而窄的疏水通道，其中包含一个结合的n-十二烷基- n， n-二甲胺- n-氧化物洗涤剂分子。单通道电导实验表明，Omp W在平面脂质双分子层中起离子通道的作用。加入n-十二烷基- n， n-二甲胺- n-氧化物可阻断通道活性。综上所述，这些数据表明Omp W家族的成员可能参与了小疏水分子在细菌外膜上的运输。
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 we have determined the crystal structure of E. coli OmpW to 2.7-angstrom 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 Omp W 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 Omp W family could be involved in the transport of small hydrophobic molecules across the bacterial outer membrane.