1ASZ

THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION

1ASZ の概要

• エントリーDOI: 10.2210/pdb1asz/pdb
• 分子名称: T-RNA (75-MER), ASPARTYL-tRNA SYNTHETASE, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: complex (aminoacyl-trna synthase-trna), complex (aminoacyl-trna synthase-trna) complex, complex (aminoacyl-trna synthase/trna)
• 由来する生物種: Saccharomyces cerevisiae
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 161430.60

構造登録者

Cavarelli, J.,Rees, B.,Thierry, J.C.,Moras, D. (登録日: 1995-01-19, 公開日: 1995-05-08, 最終更新日: 2024-02-07)

主引用文献

Cavarelli, J.,Eriani, G.,Rees, B.,Ruff, M.,Boeglin, M.,Mitschler, A.,Martin, F.,Gangloff, J.,Thierry, J.C.,Moras, D.
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction.
EMBO J., 13:327-337, 1994

PubMed Abstract: The crystal structures of the various complexes formed by yeast aspartyl-tRNA synthetase (AspRS) and its substrates provide snapshots of the active site corresponding to different steps of the aminoacylation reaction. Native crystals of the binary complex tRNA-AspRS were soaked in solutions containing the two other substrates, ATP (or its analog AMPPcP) and aspartic acid. When all substrates are present in the crystal, this leads to the formation of the aspartyl-adenylate and/or the aspartyl-tRNA. A class II-specific pathway for the aminoacylation reaction is proposed which explains the known functional differences between the two classes while preserving a common framework. Extended signature sequences characteristic of class II aaRS (motifs 2 and 3) constitute the basic functional unit. The ATP molecule adopts a bent conformation, stabilized by the invariant Arg531 of motif 3 and a magnesium ion coordinated to the pyrophosphate group and to two class-invariant acidic residues. The aspartic acid substrate is positioned by a class II invariant acidic residue, Asp342, interacting with the amino group and by amino acids conserved in the aspartyl synthetase family. The amino acids in contact with the substrates have been probed by site-directed mutagenesis for their functional implication.

PubMed: 8313877

実験手法

X-RAY DIFFRACTION (3 Å)