4Q2X

Crystal structure of Arginyl-tRNA synthetase complexed with L-canavanine

Summary for 4Q2X

• Entry DOI: 10.2210/pdb4q2x/pdb
• Related: 4Q2T 4Q2Y
• Descriptor: Arginine--tRNA ligase, cytoplasmic, L-CANAVANINE (3 entities in total)
• Functional Keywords: high region, aminoacyl-trna synthetase, atp binding, arginine binding, trna binding, ligase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P54136
• Total number of polymer chains: 2
• Total formula weight: 139047.80

Authors

Kim, H.S.,Jo, C.H.,Cha, S.Y.,Han, A.R.,Hwang, K.Y. (deposition date: 2014-04-10, release date: 2014-07-23, Last modification date: 2023-11-15)

Primary citation

Kim, H.S.,Cha, S.Y.,Jo, C.H.,Han, A.R.,Hwang, K.Y.
The crystal structure of arginyl-tRNA synthetase from Homo sapiens
Febs Lett., 588:2328-2334, 2014

PubMed 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.

PubMed: 24859084
DOI: 10.1016/j.febslet.2014.05.027

Experimental method

X-RAY DIFFRACTION (2.798 Å)