1ATI

CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

1ATI の概要

• エントリーDOI: 10.2210/pdb1ati/pdb
• 分子名称: GLYCYL-TRNA SYNTHETASE, GLYCYL-tRNA SYNTHETASE, ... (4 entities in total)
• 機能のキーワード: protein biosynthesis, ligase, synthetase, aminoacyl-trna synthetase
• 由来する生物種: Thermus thermophilus; 詳細
• 細胞内の位置: Cytoplasm: P56206
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 120874.53

構造登録者

Logan, D.T.,Mazauric, M.-H.,Kern, D.,Moras, D. (登録日: 1996-04-23, 公開日: 1997-07-07, 最終更新日: 2024-02-07)

主引用文献

Logan, D.T.,Mazauric, M.H.,Kern, D.,Moras, D.
Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus.
EMBO J., 14:4156-4167, 1995

PubMed Abstract: The sequence and crystal structure at 2.75 A resolution of the homodimeric glycyl-tRNA synthetase from Thermus thermophilus, the first representative of the last unknown class II synthetase subgroup, have been determined. The three class II synthetase sequence motifs are present but the structure was essential for identification of motif 1, which does not possess the proline previously believed to be an essential class II invariant. Nevertheless, crucial contacts with the active site of the other monomer involving motif 1 are conserved and a more comprehensive description of class II now becomes possible. Each monomer consists of an active site strongly resembling that of the aspartyl and seryl enzymes, a C-terminal anticodon recognition domain of 100 residues and a third domain unusually inserted between motifs 1 and 2 almost certainly interacting with the acceptor arm of tRNA(Gly). The C-terminal domain has a novel five-stranded parallel-antiparallel beta-sheet structure with three surrounding helices. The active site residues most probably responsible for substrate recognition, in particular in the Gly binding pocket, can be identified by inference from aspartyl-tRNA synthetase due to the conserved nature of the class II active site.

PubMed: 7556056

実験手法

X-RAY DIFFRACTION (2.75 Å)