Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition.
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 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.
Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Kelei
K
Bi
Yueting
Y
Zheng
Feng
F
Gao
Jianshu
J
Dong
Jiangyun
J
Wang
Yi
Y
Wang
Weimin
W
Gong
D001120:Arginine / Q000737:chemistry; D001126:Arginine-tRNA Ligase / Q000737:chemistry*; D001665:Binding Sites; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D008024:Ligands; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D011487:Protein Conformation; D012343:RNA, Transfer / Q000737:chemistry; D013329:Structure-Activity Relationship
D008024:Ligands; D012343:RNA, Transfer; D001120:Arginine; D001126:Arginine-tRNA Ligase