脂质双分子层中水通道蛋白Z的固态核磁共振化学位移归属
Solid-state NMR chemical shift assignments of aquaporin Z in lipid bilayers.
作者信息
Xie Huayong, Zhao Yongxiang, Wang Jing, Zhang Zhengfeng, Yang Jun
机构信息
National Center for Magnetic Resonance in Wuhan, Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, People's Republic of China.
University of Chinese Academy of Sciences, Beijing, 100049, People's Republic of China.
出版信息
Biomol NMR Assign. 2018 Oct;12(2):323-328. doi: 10.1007/s12104-018-9832-5. Epub 2018 Jun 25.
Aquaporin Z is the first identified prokaryotic water channel in Escherichia coli with a high water permeability and strict substrate selectivity. Here we report nearly complete (94% of amino acid residues) C and N chemical shift assignments of AqpZ reconstituted in the lipid bilayers using a set of 2D and 3D magic angle spinning solid-state NMR spectra. Secondary structure of AqpZ predicted from chemical shift assignments is generally similar to that of X-ray structure with a number of differences in loop and near-loop regions. The BMRB accession number of the assignments is 27244.
水通道蛋白Z是在大肠杆菌中首次鉴定出的原核生物水通道，具有高水渗透性和严格的底物选择性。在此，我们报告了使用一组二维和三维魔角旋转固态核磁共振谱对重构于脂质双层中的水通道蛋白Z进行的近乎完整的（94%的氨基酸残基）碳和氮化学位移归属。根据化学位移归属预测的水通道蛋白Z的二级结构与X射线结构总体相似，但在环区和近环区存在一些差异。这些归属的BMRB登录号为27244。
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