2HZ7

Crystal structure of the Glutaminyl-tRNA synthetase from Deinococcus radiodurans

2HZ7 の概要

• エントリーDOI: 10.2210/pdb2hz7/pdb
• 分子名称: Glutaminyl-tRNA synthetase (2 entities in total)
• 機能のキーワード: rossmann fold, glnrs core, class i aminoacyl-trna synthetase, ligase
• 由来する生物種: Deinococcus radiodurans
• 細胞内の位置: Cytoplasm : P56926
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 93460.67

構造登録者

Deniziak, M.,Sauter, C.,Becker, H.D.,Paulus, C.,Giege, R.,Kern, D. (登録日: 2006-08-08, 公開日: 2007-04-24, 最終更新日: 2023-08-30)

主引用文献

Deniziak, M.,Sauter, C.,Becker, H.D.,Paulus, C.A.,Giege, R.,Kern, D.
Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation
Nucleic Acids Res., 35:1421-1431, 2007

PubMed Abstract: Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein present in various organisms and part of it is present in the C-terminal end of the GatB subunit of GatCAB, a partner of the indirect pathway of Gln-tRNA(Gln) formation. To analyze the peculiarities of the structure-function relationship of this GlnRS related to the Yqey domain, a structure of the protein was solved from crystals diffracting at 2.3 A and a docking model of the synthetase complexed to tRNA(Gln) constructed. The comparison of the modeled complex with the structure of the E. coli complex reveals that all residues of E. coli GlnRS contacting tRNA(Gln) are conserved in D. radiodurans GlnRS, leaving the functional role of the Yqey domain puzzling. Kinetic investigations and tRNA-binding experiments of full length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved in tRNA(Gln) recognition. They demonstrate that Yqey plays the role of an affinity-enhancer of GlnRS for tRNA(Gln) acting only in cis. However, the presence of Yqey in free state in organisms lacking GlnRS, suggests that this domain may exert additional cellular functions.

PubMed: 17284460
DOI: 10.1093/nar/gkl1164

実験手法

X-RAY DIFFRACTION (2.3 Å)