1IRX

Crystal structure of class I lysyl-tRNA synthetase

1IRX の概要

• エントリーDOI: 10.2210/pdb1irx/pdb
• 分子名称: lysyl-tRNA synthetase, ZINC ION (3 entities in total)
• 機能のキーワード: beta sandwitch, zinc-binding structure, rossmann fold, alpha-helix cage, riken structural genomics/proteomics initiative, rsgi, structural genomics, ligase
• 由来する生物種: Pyrococcus horikoshii
• 細胞内の位置: Cytoplasm: O57963
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 123574.44

構造登録者

Nureki, O.,Terada, T.,Ishitani, R.,Ambrogelly, A.,Ibba, M.,Soll, D.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2001-10-25, 公開日: 2002-04-17, 最終更新日: 2023-12-27)

主引用文献

Terada, T.,Nureki, O.,Ishitani, R.,Ambrogelly, A.,Ibba, M.,Soll, D.,Yokoyama, S.
Functional convergence of two lysyl-tRNA synthetases with unrelated topologies.
Nat.Struct.Biol., 9:257-262, 2002

PubMed Abstract: Lysyl-tRNA can be synthesized by both a class I (LysRS-I) and a class II (LysRS-II) lysyl-tRNA synthetase. The crystal structure of LysRS-I from Pyrococcus horikoshii at 2.6 A resolution reveals extensive similarity with glutamyl-tRNA synthetase (GluRS). A comparison of the structures of LysRS-I and LysRS-II in complex with lysine shows that both enzymes use similar strategies for substrate recognition within unrelated active site topologies. A docking model based upon the GluRS-tRNA complex suggests how LysRS-I and LysRS-II can recognize the same molecular determinants in tRNALys, as shown by biochemical results, while approaching the acceptor helix of the tRNA from opposite sides.

PubMed: 11887185
DOI: 10.1038/nsb777

実験手法

X-RAY DIFFRACTION (2.6 Å)