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Publication Abstract from PubMed

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 S-transferase (GST) domains from AIMP2 and glutamyl-prolyl-tRNA synthetase (AIMP2GST and EPRSGST, respectively). While AIMP2GST and EPRSGST interact via conventional GST heterodimerization, DRS strongly interacts with AIMP2GST via hydrogen bonds between the alpha7-beta9 loop of DRS and the beta2-alpha2 loop of AIMP2GST, where Ser156 of AIMP2GST is essential for the assembly. Structural analyses of DRS-AIMP2GST-EPRSGST reveal its pivotal architecture in the MSC and provide valuable insights into the overall assembly and conditionally required disassembly of the MSC.

The DRS-AIMP2-EPRS subcomplex acts as a pivot in the multi-tRNA synthetase complex.,Hahn H, Park SH, Kim HJ, Kim S, Han BW IUCrJ. 2019 Aug 24;6(Pt 5):958-967. doi: 10.1107/S2052252519010790. eCollection, 2019 Sep 1. PMID:31576228^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.