4Q2T: Crystal structure of Arginyl-tRNA synthetase complexed with L-arginine

Citation:
Abstract
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.
PDB ID: 4Q2TDownload
MMDB ID: 121756
PDB Deposition Date: 2014/4/9
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 4Q2T: monomeric; determined by author and by software (PISA)
Molecular Components in 4Q2T
Label Count Molecule
Protein (1 molecule)
1
Arginine--trna Ligase, Cytoplasmic(Gene symbol: RARS)
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

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