1D2D

Hamster EprS second repeated element. NMR, 5 structures

1D2D の概要

• エントリーDOI: 10.2210/pdb1d2d/pdb
• 関連するPDBエントリー: 1R1B
• 分子名称: TRNA SYNTHETASE (1 entity in total)
• 機能のキーワード: trna synthetase (ligase), protein transcription, ligase
• 由来する生物種: Cricetulus griseus (Chinese hamster)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6721.82

構造登録者

Cahuzac, B.,Berthonneau, E.,Birlirakis, N.,Guittet, E.,Mirande, M. (登録日: 1999-09-23, 公開日: 2000-05-24, 最終更新日: 2024-05-22)

主引用文献

Cahuzac, B.,Berthonneau, E.,Birlirakis, N.,Guittet, E.,Mirande, M.
A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases.
EMBO J., 19:445-452, 2000

PubMed Abstract: Aminoacyl-tRNA synthetases of higher eukaryotes possess polypeptide extensions in contrast to their prokaryotic counterparts. These extra domains of poorly understood function are believed to be involved in protein-protein or protein-RNA interactions. Here we showed by gel retardation and filter binding experiments that the repeated units that build the linker region of the bifunctional glutamyl-prolyl-tRNA synthetase had a general RNA-binding capacity. The solution structure of one of these repeated motifs was also solved by NMR spectroscopy. One repeat is built around an antiparallel coiled-coil. Strikingly, the conserved lysine and arginine residues form a basic patch on one side of the structure, presenting a suitable docking surface for nucleic acids. Therefore, this repeated motif may represent a novel type of general RNA-binding domain appended to eukaryotic aminoacyl-tRNA synthetases to serve as a cis-acting tRNA-binding cofactor.

PubMed: 10654942
DOI: 10.1093/emboj/19.3.445

実験手法

SOLUTION NMR