Ontology highlight
ABSTRACT:
SUBMITTER: Bi K
PROVIDER: S-EPMC3956977 | biostudies-literature | 2014 Feb
REPOSITORIES: biostudies-literature
Bi Kelei K Zheng Yueting Y Gao Feng F Dong Jianshu J Wang Jiangyun J Wang Yi Y Gong Weimin W
Protein & cell 20140130 2
The arginyl-tRNA synthetase (ArgRS) catalyzes the esterification reaction between L-arginine and its cognate tRNA(Arg). 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 rep ...[more]