The crystal structure of arginyl-tRNA synthetase from Homo sapiens

Hyun Sook Kim, So Young Cha, Chang Hwa Jo, Ahreum Han, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)


Arginyl-tRNA synthetase (ArgRS) is a tRNA-binding protein that catalyzes the esterification of l-arginine to its cognate tRNA. l-Canavanine, a structural analog of l-arginine, has recently been studied as an anticancer agent. Here, we determined the crystal structures of the apo, l-arginine-complexed, and l-canavanine-complexed forms of the cytoplasmic free isoform of human ArgRS (hArgRS). Similar interactions were formed upon binding to l-canavanine or l-arginine, but the interaction between Tyr312 and the oxygen of the oxyguanidino group was a little bit different. Detailed conformational changes that occur upon substrate binding were explained. The hArgRS structure was also compared with previously reported homologue structures. The results presented here may provide a basis for the design of new anticancer drugs, such as l-canavanine analogs.

Original languageEnglish
Pages (from-to)2328-2334
Number of pages7
JournalFEBS Letters
Issue number14
Publication statusPublished - 2014 Jun 27

Bibliographical note

Funding Information:
We thank the staff of beamline 4A at the Pohang Accelerator Laboratory and beamline BL1A at the Photon Factory for technical support (2012G189). We are also grateful to the staff at the Korean Basic Science Institute (Daejeon, Korea) for the use of a mosquito crystallization robot and the Rigaku MicroMax-007HF X-ray generator. This work was supported by grants from the National Research Foundation of Korea ( 2013-044795 ).


  • Arginyl-tRNA synthetase
  • Enzyme Commission number (
  • Rossmann fold
  • l-Arginine
  • l-Canavanine

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


Dive into the research topics of 'The crystal structure of arginyl-tRNA synthetase from Homo sapiens'. Together they form a unique fingerprint.

Cite this