1HTT

HISTIDYL-TRNA SYNTHETASE

Summary for 1HTT

• Entry DOI: 10.2210/pdb1htt/pdb
• Descriptor: HISTIDYL-TRNA SYNTHETASE, HISTIDINE, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: complex (trna synthetase-his-adenylate), aminoacyl-trna synthase, ligase, synthetase, complex (trna synthetase-his-adenylate) complex, complex (trna synthetase/his-adenylate)
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 189830.02

Authors

Arnez, J.G.,Harris, D.C.,Mitschler, A.,Rees, B.,Francklyn, C.S.,Moras, D. (deposition date: 1996-03-09, release date: 1997-01-27, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)