Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition

作     者：Kelei Bi Yueting Zheng Feng G"ao Jianshu Dong Jiangyun Wang Yi Wang Weimin Gong 

作者机构：Laboratory of Non-coding RNA Institute of Biophysics Chinese Academy of Sciences 

出 版 物：《Protein & Cell》 (蛋白质与细胞(英文))

年 卷 期：2014年第5卷第2期

页      面：151-159页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学] 

基　　金：funded by the National Basic Research Program (973 Program) (No. 2010CB912301) the Chinese Academy of Sciences (KSCX2-EW-G-7-2) the National Natural Science Foundation of China (Grant No. 91219202) 

主　　题：arginyl-tRNA synthetase amino acyl-tRNA synthetase isothermal titration calorimetry site-directed mutation X-ray crystal structure E. coli 

摘      要：The arginyl-tRNA synthetase(ArgRS) catalyzes the esterification reaction between L-arginine and its cognate tRNAArg. Previously reported structures of ArgRS shed considerable light on the tRNA recognition mechanism, while the aspect of amino acid binding in ArgRS remains largely unexplored. Here we report the first crystal structure of E. coli ArgRS(eArgRS) complexed with L-arginine, and a series of mutational studies using isothermal titration calorimetry(ITC). Combined with previously reported work on ArgRS, our results elucidated the structural and functional roles of a series of important residues in the active site, which furthered our understanding of this unique enzyme.