1BS2

YEAST ARGINYL-TRNA SYNTHETASE

1BS2 の概要

• エントリーDOI: 10.2210/pdb1bs2/pdb
• 分子名称: PROTEIN (ARGINYL-TRNA SYNTHETASE), ARGININE (3 entities in total)
• 機能のキーワード: ligase, aminoacyl-trna synthetase, protein biosynthesis
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm : Q05506
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 69793.08

構造登録者

Cavarelli, J.,Delagouute, B.,Eriani, G.,Gangloff, J.,Moras, D. (登録日: 1998-08-31, 公開日: 1999-08-27, 最終更新日: 2024-03-13)

主引用文献

Cavarelli, J.,Delagoutte, B.,Eriani, G.,Gangloff, J.,Moras, D.
L-arginine recognition by yeast arginyl-tRNA synthetase.
EMBO J., 17:5438-5448, 1998

PubMed Abstract: The crystal structure of arginyl-tRNA synthetase (ArgRS) from Saccharomyces cerevisiae, a class I aminoacyl-tRNA synthetase (aaRS), with L-arginine bound to the active site has been solved at 2.75 A resolution and refined to a crystallographic R-factor of 19.7%. ArgRS is composed predominantly of alpha-helices and can be divided into five domains, including the class I-specific active site. The N-terminal domain shows striking similarity to some completely unrelated proteins and defines a module which should participate in specific tRNA recognition. The C-terminal domain, which is the putative anticodon-binding module, displays an all-alpha-helix fold highly similar to that of Escherichia coli methionyl-tRNA synthetase. While ArgRS requires tRNAArg for the first step of the aminoacylation reaction, the results show that its presence is not a prerequisite for L-arginine binding. All H-bond-forming capability of L-arginine is used by the protein for the specific recognition. The guanidinium group forms two salt bridge interactions with two acidic residues, and one H-bond with a tyrosine residue; these three residues are strictly conserved in all ArgRS sequences. This tyrosine is also conserved in other class I aaRS active sites but plays several functional roles. The ArgRS structure allows the definition of a new framework for sequence alignments and subclass definition in class I aaRSs.

PubMed: 9736621
DOI: 10.1093/emboj/17.18.5438

実験手法

X-RAY DIFFRACTION (2.75 Å)