Structure of the outer membrane protein A transmembrane domain
Structure of the outer membrane protein A transmembrane domain
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DOI：
10.1038/2983
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发表时间：
1998-11-01
期刊：
影响因子：
--
通讯作者：
Schulz, GE
中科院分区：
文献类型：
--
作者：
Pautsch, A;Schulz, GE
大肠杆菌外膜蛋白A（OmpA）是膜蛋白折叠领域深入研究的一个例子。我们已经通过X射线衍射分析确定了由残基1-171组成的OmpA跨膜结构域的结构，分辨率为2.5埃。它由一个规则的、延伸的八链β-桶组成，并且看起来像一个具有大的充满水的空腔的反胶束，但不形成孔。令人惊讶的是，这些空腔在进化过程中似乎高度保守。该结构证实了所有外膜蛋白都由β桶组成的概念。该结构构成β-桶膜锚，其看起来是内膜的单链α-螺旋锚的外膜等同物。
The outer membrane protein A of Escherichia coli (OmpA) is an intensely studied example in the field of membrane protein folding. We have determined the structure of the OmpA transmembrane domain consisting of residues 1-171, by X-ray diffraction analysis, to a resolution of 2.5 Angstrom. It consists of a regular, extended eight-stranded beta-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. Surprisingly, the cavities seem to be highly conserved during evolution. The structure corroborates the concept that all outer membrane proteins consist of beta-barrels. The structure constitutes a beta-barrel membrane anchor that appears to be the outer membrane equivalent of the single-chain alpha-helix anchor of the inner membrane.