1H, 13C and 15N NMR assignments of cyclophilin LRT2 (OsCYP2) from rice
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 1H, 13C, 15N 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.
KeywordsNMR resonance assignments TALOS-N prediction Rice cyclophilin Lateral root development Protein chemical shift assignment
This investigation was supported by the National Science Foundation (MCB-1615350) and through graduate student training grant support to LAA by the National Institutes of Health (2T32GM008267).
- Goddard TD, Kneller DG SPARKY 3. University of California, San FranciscoGoogle Scholar
- Kumari S, Singh P, Singla-Pareek SL, Pareek A (2009) Heterologous expression of a salinity and developmentally regulated rice cyclophilin gene (OsCyp2) in E. coli and S. cerevisiae confers tolerance towards multiple abiotic stresses. Mol Biotechnol 42:195–204. https://doi.org/10.1007/s12033-009-9153-0 CrossRefGoogle Scholar