5ZDK

Crystal Structure Analysis of TtQRS in complex with ATP

5ZDK の概要

• エントリーDOI: 10.2210/pdb5zdk/pdb
• 関連するPDBエントリー: 1QRU
• 分子名称: Glutamine--tRNA ligase, ADENOSINE-5'-TRIPHOSPHATE, CESIUM ION, ... (6 entities in total)
• 機能のキーワード: glnrs, qrs, ligase, synthetase
• 由来する生物種: Thermus thermophilus HB8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64451.75

構造登録者

Mutharasappan, N.,Jain, V.,Sharma, A.,Manickam, Y.,Jeyaraman, J. (登録日: 2018-02-23, 公開日: 2018-12-05, 最終更新日: 2023-11-22)

主引用文献

Nachiappan, M.,Jain, V.,Sharma, A.,Yogavel, M.,Jeyakanthan, J.
Structural and functional analysis of Glutaminyl-tRNA synthetase (TtGlnRS) from Thermus thermophilus HB8 and its complexes
Int. J. Biol. Macromol., 120:1379-1386, 2018

PubMed Abstract: Aminoacyl-tRNA synthetases (AaRSs) are vital enzymes for translation of proteins in cells. AaRSs catalyse the esterification of a specific amino acid to corresponding tRNAs to form an aminoacyl-tRNA that is used in ribosome-based protein synthesis. We focused on Glutaminyl tRNA synthetase (GlnRS) enzyme from the extreme thermophile Thermus thermophilus for structural studies. Our thermal shift assays show binding of enzyme substrates L-Gln and ATP as well as of various metals including cesium. We resolved crystal structures of apo-GlnRS as well as those in complex with AMP and ATP at 2.8 Å, 2.4 Å and 2.6 Å respectively. The bound cesium was found at the site of magnesium that typically binds to GlnRS. High structural conservation was evident in the Thermus thermophilus GlnRS when compared to those from Escherichia coli GlnRS.

PubMed: 30248426
DOI: 10.1016/j.ijbiomac.2018.09.115

実験手法

X-RAY DIFFRACTION (2.45 Å)