7F6W

Crystal structure of Saccharomyces cerevisiae lysyl-tRNA Synthetase

7F6W の概要

• エントリーDOI: 10.2210/pdb7f6w/pdb
• 分子名称: Lysine--tRNA ligase, 5'-O-[(L-LYSYLAMINO)SULFONYL]ADENOSINE, 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE, ... (4 entities in total)
• 機能のキーワード: lysine-trna ligase; protein translation enzyme, ligase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61537.91

構造登録者

Wu, S.,Li, P.,Hei, Z.,Zheng, L.,Wang, J.,Fang, P. (登録日: 2021-06-26, 公開日: 2022-02-16, 最終更新日: 2023-11-29)

主引用文献

Wu, S.,Zheng, L.,Hei, Z.,Zhou, J.B.,Li, G.,Li, P.,Wang, J.,Ali, H.,Zhou, X.L.,Wang, J.,Fang, P.
Human lysyl-tRNA synthetase evolves a dynamic structure that can be stabilized by forming complex.
Cell.Mol.Life Sci., 79:128-128, 2022

PubMed Abstract: The evolutionary necessity of aminoacyl-tRNA synthetases being associated into complex is unknown. Human lysyl-tRNA synthetase (LysRS) is one component of the multi-tRNA synthetase complex (MSC), which is not only critical for protein translation but also involved in multiple cellular pathways such as immune response, cell migration, etc. Here, combined with crystallography, CRISPR/Cas9-based genome editing, biochemistry, and cell biology analyses, we show that the structures of LysRSs from metazoan are more dynamic than those from single-celled organisms. Without the presence of MSC scaffold proteins, such as aminoacyl-tRNA synthetase complex-interacting multifunctional protein 2 (AIMP2), human LysRS is free from the MSC. The interaction with AIMP2 stabilizes the closed conformation of LysRS, thereby protects the essential aminoacylation activity under stressed conditions. Deleting AIMP2 from the human embryonic kidney 293 cells leads to retardation in cell growth in nutrient deficient mediums. Together, these results suggest that the evolutionary emergence of the MSC in metazoan might be to protect the aminoacyl-tRNA synthetase components from being modified or recruited for use in other cellular pathways.

PubMed: 35133502
DOI: 10.1007/s00018-022-04158-9

実験手法

X-RAY DIFFRACTION (2.607 Å)