6IY6

Crystal structure of human cytosolic aspartyl-tRNA synthetase (DRS) in complex with glutathion-S transferase (GST) domains from Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (AIMP2) and glutamyl-prolyl-tRNA synthetase (EPRS)

Summary for 6IY6

• Entry DOI: 10.2210/pdb6iy6/pdb
• Descriptor: Aspartate--tRNA ligase, cytoplasmic, Aminoacyl tRNA synthase complex-interacting multifunctional protein 2, Bifunctional glutamate/proline--tRNA ligase, ... (6 entities in total)
• Functional Keywords: aminoacyl-trna transferase glutathion-s transferase domain, translation
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 12
• Total formula weight: 401385.13

Authors

Park, S.H.,Hahn, H.,Han, B.W. (deposition date: 2018-12-13, release date: 2019-09-11, Last modification date: 2023-11-22)

Primary citation

Hahn, H.,Park, S.H.,Kim, H.J.,Kim, S.,Han, B.W.
The DRS-AIMP2-EPRS subcomplex acts as a pivot in the multi-tRNA synthetase complex.
Iucrj, 6:958-967, 2019

PubMed Abstract: Aminoacyl-tRNA synthetases (ARSs) play essential roles in protein biosynthesis as well as in other cellular processes, often using evolutionarily acquired domains. For possible cooperativity and synergistic effects, nine ARSs assemble into the multi-tRNA synthetase complex (MSC) with three scaffold proteins: aminoacyl-tRNA synthetase complex-interacting multifunctional proteins 1, 2 and 3 (AIMP1, AIMP2 and AIMP3). X-ray crystallographic methods were implemented in order to determine the structure of a ternary subcomplex of the MSC comprising aspartyl-tRNA synthetase (DRS) and two glutathione -transferase (GST) domains from AIMP2 and glutamyl-prolyl-tRNA synthetase (AIMP2 and EPRS, respectively). While AIMP2 and EPRS interact via conventional GST heterodimerization, DRS strongly interacts with AIMP2 via hydrogen bonds between the α7-β9 loop of DRS and the β2-α2 loop of AIMP2, where Ser156 of AIMP2 is essential for the assembly. Structural analyses of DRS-AIMP2-EPRS reveal its pivotal architecture in the MSC and provide valuable insights into the overall assembly and conditionally required disassembly of the MSC.

PubMed: 31576228
DOI: 10.1107/S2052252519010790

Experimental method

X-RAY DIFFRACTION (3.6 Å)