Acevedo Lucila Andrea, Nicholson Linda K
Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, 14853, USA.
Biomol NMR Assign. 2018 Apr;12(1):171-174. doi: 10.1007/s12104-018-9803-x. Epub 2018 Jan 20.
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, C, N 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.
亲环蛋白是催化脯氨酰 - 肽键异构化的酶，存在于原核生物和真核生物中。LRT2（也称为OsCYP2）是水稻（Oryza sativa）中的一种亲环蛋白，在侧根发育和胁迫耐受性方面具有重要作用。LRT2由172个氨基酸组成，分子量为18.3 kDa。在此，我们在pH 6.7和298 K条件下，使用多种二维和三维异核NMR实验，报道了LRT2蛋白中H、C、N的主链和侧链共振归属。我们的化学位移数据分析预测其二级结构类似于胞质小麦亲环蛋白TaCypA - 1，序列同一性为87.7%。这些归属将有助于对该酶的功能和结构进行NMR研究的进一步分析。
