期刊
IUCRJ
卷 6, 期 -, 页码 958-967出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2052252519010790
关键词
aspartyl-tRNA synthetase; aminoacyl-tRNA synthetase complex-interacting multifunctional protein 2; glutamyl-prolyl-tRNA synthetase; multi-tRNA synthetase complex
资金
- National Research Foundation of Korea (NRF) - Ministry of Science and ICT of Republic of Korea [NRF-2013M-3A6A-4043695, NRF-2011-0030001]
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 (AIMP2(GST) and EPRSGST, respectively). While AIMP2(GST) and EPRSGST interact via conventional GST heterodimerization, DRS strongly interacts with AIMP2(GST) via hydrogen bonds between the alpha 7-beta 9 loop of DRS and the beta 2-alpha 2 loop of AIMP2(GST), where Ser156 of AIMP2(GST) is essential for the assembly. Structural analyses of DRS-AIMP2(GST)-EPRSGST reveal its pivotal architecture in the MSC and provide valuable insights into the overall assembly and conditionally required disassembly of the MSC.
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