1GLN

ARCHITECTURES OF CLASS-DEFINING AND SPECIFIC DOMAINS OF GLUTAMYL-TRNA SYNTHETASE

1GLN の概要

• エントリーDOI: 10.2210/pdb1gln/pdb
• 分子名称: GLUTAMYL-TRNA SYNTHETASE (2 entities in total)
• 機能のキーワード: riken structural genomics/proteomics initiative, rsgi, structural genomics, aminoacyl-trna synthase
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cytoplasm : P27000
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53979.73

構造登録者

Nureki, O.,Vassylyev, D.G.,Katayanagi, K.,Shimizu, T.,Sekine, S.,Kigawa, T.,Miyazawa, T.,Yokoyama, S.,Morikawa, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 1994-07-20, 公開日: 1995-10-15, 最終更新日: 2024-02-07)

主引用文献

Nureki, O.,Vassylyev, D.G.,Katayanagi, K.,Shimizu, T.,Sekine, S.,Kigawa, T.,Miyazawa, T.,Yokoyama, S.,Morikawa, K.
Architectures of class-defining and specific domains of glutamyl-tRNA synthetase.
Science, 267:1958-1965, 1995

PubMed Abstract: The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and refined at 2.5 A resolution. The amino-terminal half of GluRS shows a geometrical similarity with that of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) of the same subclass in class I, comprising the class I-specific Rossmann fold domain and the intervening subclass-specific alpha/beta domain. These domains were found to have two GluRS-specific, secondary-structure insertions, which then participated in the specific recognition of the D and acceptor stems of tRNA(Glu) as indicated by mutagenesis analyses based on the docking properties of GluRS and tRNA. In striking contrast to the beta-barrel structure of the GlnRS carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an all-alpha-helix architecture, an alpha-helix cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition.

PubMed: 7701318

実験手法

X-RAY DIFFRACTION (2.5 Å)