4OBY

Crystal Structure of E.coli Arginyl-tRNA Synthetase and Ligand Binding Studies Revealed Key Residues in Arginine Recognition

4OBY の概要

• エントリーDOI: 10.2210/pdb4oby/pdb
• 分子名称: Arginine--tRNA ligase, ARGININE (3 entities in total)
• 機能のキーワード: ligase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65024.10

構造登録者

Bi, K.,Zheng, Y.,Dong, J.,Gao, F.,Wang, J.,Wang, Y.,Gong, W. (登録日: 2014-01-08, 公開日: 2014-02-12, 最終更新日: 2023-09-20)

主引用文献

Bi, K.,Zheng, Y.,Gao, F.,Dong, J.,Wang, J.,Wang, Y.,Gong, W.
Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition.
Protein Cell, 5:151-159, 2014

PubMed Abstract: 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.

PubMed: 24474195
DOI: 10.1007/s13238-013-0012-1

実験手法

X-RAY DIFFRACTION (2.574 Å)