1HTT

HISTIDYL-TRNA SYNTHETASE

1HTT の概要

• エントリーDOI: 10.2210/pdb1htt/pdb
• 分子名称: HISTIDYL-TRNA SYNTHETASE, HISTIDINE, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: complex (trna synthetase-his-adenylate), aminoacyl-trna synthase, ligase, synthetase, complex (trna synthetase-his-adenylate) complex, complex (trna synthetase/his-adenylate)
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 189830.02

構造登録者

Arnez, J.G.,Harris, D.C.,Mitschler, A.,Rees, B.,Francklyn, C.S.,Moras, D. (登録日: 1996-03-09, 公開日: 1997-01-27, 最終更新日: 2024-02-07)

主引用文献

Arnez, J.G.,Harris, D.C.,Mitschler, A.,Rees, B.,Francklyn, C.S.,Moras, D.
Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate.
EMBO J., 14:4143-4155, 1995

PubMed Abstract: The crystal structure at 2.6 A of the histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate has been determined. The enzyme is a homodimer with a molecular weight of 94 kDa and belongs to the class II of aminoacyl-tRNA synthetases (aaRS). The asymmetric unit is composed of two homodimers. Each monomer consists of two domains. The N-terminal catalytic core domain contains a six-stranded antiparallel beta-sheet sitting on two alpha-helices, which can be superposed with the catalytic domains of yeast AspRS, and GlyRS and SerRS from Thermus thermophilus with a root-mean-square difference on the C alpha atoms of 1.7-1.9 A. The active sites of all four monomers are occupied by histidyl-adenylate, which apparently forms during crystallization. The 100 residue C-terminal alpha/beta domain resembles half of a beta-barrel, and provides an independent domain oriented to contact the anticodon stem and part of the anticodon loop of tRNA(His). The modular domain organization of histidyl-tRNA synthetase reiterates a repeated theme in aaRS, and its structure should provide insight into the ability of certain aaRS to aminoacylate minihelices and other non-tRNA molecules.

PubMed: 7556055

実験手法

X-RAY DIFFRACTION (2.6 Å)