Download MendeleyCrystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate.
Arnez, J.G., Harris, D.C., Mitschler, A., Rees, B., Francklyn, C.S., Moras, D.(1995) EMBO J 14: 4143-4155
- PubMed: 7556055
- DOI: https://doi.org/10.1002/j.1460-2075.1995.tb00088.x
- Primary Citation of Related Structures:
1HTT - 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.
Organizational Affiliation:
INSERM/ULP BP 163, Illkirch, France.
