Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
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DOI：
10.1038/86214
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发表时间：
2001-04-01
期刊：
影响因子：
--
通讯作者：
Tamm, LK
中科院分区：
文献类型：
--
作者：
Arora, A;Abildgaard, F;Tamm, LK
我们已经确定了19 kDa（177个残基）的跨膜结构域的大肠杆菌十二烷基磷酸胆碱（DPC）胶束的外膜蛋白A在溶液中使用异频NMR的三维倍。该结构由在周质侧上通过紧转弯连接的八链β-桶和在细胞外侧上的较大的移动的环组成。X射线衍射结果表明，DPC胶束中的桶形结构与正辛基四氧杂环己烷（C_8E_4）胶束中的桶形结构相似。此外，从NMR动态实验的数据揭示了梯度的构象灵活性的结构，可能有助于这种蛋白质的膜通道功能。
We have determined the three-dimensional fold of the 19 kDa (177 residues) transmembrane domain of the outer membrane protein A of Escherichia coli dodecylphosphocholine (DPC) micelles in solution using heteronuclear NMR. The structure consists of an eight-stranded beta -barrel connected by tight turns on the periplasmic side and larger mobile loops on the extracellular side. The solution structure of the barrel in DPC micelles is similar to that in n-octyltetraoxyethylene (C8E4) micelles determined by X-ray diffraction. Moreover, data from NMR dynamic experiments reveal a gradient of conformational flexibility in the structure that may contribute to the membrane channel function of this protein.