The arginyl-tRNA synthetase （ArgRS） catalyzes the esterification reaction between L-arginine and its cog- nate tRNAArg. Previously reported structures of ArgRS shed considerable light on the tRNA recognition mech- a...The arginyl-tRNA synthetase （ArgRS） catalyzes the esterification reaction between L-arginine and its cog- nate tRNAArg. Previously reported structures of ArgRS shed considerable light on the tRNA recognition mech- anism, 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 eluci- dated the structural and functional roles of a series of important residues in the active site, which furthered our understanding of this unique enzyme.展开更多
基金This project was funded by the National Basic Research Program （973 Program） （No. 2010CB912301）, the Chinese Academy of Sciences （KSCX2-EW-G-7-2） and the National Natural Science Foundation of China （Grant No. 91219202）.
文摘The arginyl-tRNA synthetase （ArgRS） catalyzes the esterification reaction between L-arginine and its cog- nate tRNAArg. Previously reported structures of ArgRS shed considerable light on the tRNA recognition mech- anism, 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 eluci- dated the structural and functional roles of a series of important residues in the active site, which furthered our understanding of this unique enzyme.
