1NYL

Unliganded glutaminyl-tRNA synthetase

1NYL の概要

• エントリーDOI: 10.2210/pdb1nyl/pdb
• 分子名称: Glutaminyl-tRNA synthetase (2 entities in total)
• 機能のキーワード: ligase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P00962
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61920.00

構造登録者

Sherlin, L.D.,Perona, J.P. (登録日: 2003-02-12, 公開日: 2003-02-25, 最終更新日: 2011-07-13)

主引用文献

Sherlin, L.D.,Perona, J.J.
tRNA-Dependent Active Site Assembly in a Class I Aminoacyl-tRNA Synthetase.
Structure, 11:591-603, 2003

PubMed Abstract: The crystal structure of ligand-free E. coli glutaminyl-tRNA synthetase (GlnRS) at 2.4 A resolution shows that substrate binding is essential to construction of a catalytically proficient active site. tRNA binding generates structural changes throughout the enzyme, repositioning key active site peptides that bind glutamine and ATP. The structure gives insight into longstanding questions regarding the tRNA dependence of glutaminyl adenylate formation, the coupling of amino acid and tRNA selectivities, and the roles of specific pathways for transmission of tRNA binding signals to the active site. Comparative analysis of the unliganded and tRNA-bound structures shows, in detail, how flexibility is built into the enzyme architecture and suggests that the induced-fit transitions are a key underlying determinant of both amino acid and tRNA specificity.

PubMed: 12737824
DOI: 10.1016/S0969-2126(03)00074-1

実験手法

X-RAY DIFFRACTION (2.6 Å)