1H, 13C and 15N NMR assignments of cyclophilin LRT2 (OsCYP2) from rice

被引:2
|
作者
Acevedo, Lucila Andrea [1 ]
Nicholson, Linda K. [1 ]
机构
[1] Cornell Univ, Dept Mol Biol & Genet, Ithaca, NY 14853 USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
NMR resonance assignments; TALOS-N prediction; Rice cyclophilin; Lateral root development; Protein chemical shift assignment;
D O I
10.1007/s12104-018-9803-x
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Cyclophilins are enzymes that catalyze the isomerization of a prolyl-peptide bond and are found in both prokaryotes and eukaryotes. LRT2 (also known as OsCYP2) is a cyclophilin in rice (Oryza sativa), that has importance in lateral root development and stress tolerance. LRT2 is 172 amino acids long and has a molecular weight of 18.3 kDa. Here, we report the backbone and sidechain resonance assignments of H-1, C-13, N-15 in the LRT2 protein using several 2D and 3D heteronuclear NMR experiments at pH 6.7 and 298 K. Our chemical shift data analysis predicts a secondary structure like the cytosolic wheat cyclophilin TaCypA-1 with 87.7% sequence identity. These assignments will be useful for further analysis in the NMR studies for function and structure of this enzyme.
引用
收藏
页码:171 / 174
页数:4
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