3AFH

Crystal structure of Thermotoga maritima nondiscriminating glutamyl-tRNA synthetase in complex with a glutamyl-AMP analog

Summary for 3AFH

• Entry DOI: 10.2210/pdb3afh/pdb
• Descriptor: Glutamyl-tRNA synthetase 2, O5'-(L-GLUTAMYL-SULFAMOYL)-ADENOSINE (3 entities in total)
• Functional Keywords: protein-substrate complex, non-discriminating glutamyl-trna synthetase, aminoacyl-trna synthetase, atp-binding, ligase, nucleotide-binding, protein biosynthesis
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm: Q9X2I8
• Total number of polymer chains: 1
• Total formula weight: 58001.03

Authors

Ito, T.,Yokoyama, S. (deposition date: 2010-03-01, release date: 2010-06-30, Last modification date: 2023-11-01)

Primary citation

Ito, T.,Kiyasu, N.,Matsunaga, R.,Takahashi, S.,Yokoyama, S.
Structure of nondiscriminating glutamyl-tRNA synthetase from Thermotoga maritima
Acta Crystallogr.,Sect.D, 66:813-820, 2010

PubMed Abstract: Aminoacyl-tRNA synthetases produce aminoacyl-tRNAs from the substrate tRNA and its cognate amino acid with the aid of ATP. Two types of glutamyl-tRNA synthetase (GluRS) have been discovered: discriminating GluRS (D-GluRS) and nondiscriminating GluRS (ND-GluRS). D-GluRS glutamylates tRNA(Glu) only, while ND-GluRS glutamylates both tRNA(Glu) and tRNA(Gln). ND-GluRS produces the intermediate Glu-tRNA(Gln), which is converted to Gln-tRNA(Gln) by Glu-tRNA(Gln) amidotransferase. Two GluRS homologues from Thermotoga maritima, TM1875 and TM1351, have been biochemically characterized and it has been clarified that only TM1875 functions as an ND-GluRS. Furthermore, the crystal structure of the T. maritima ND-GluRS, TM1875, was determined in complex with a Glu-AMP analogue at 2.0 A resolution. The T. maritima ND-GluRS contains a characteristic structure in the connective-peptide domain, which is inserted into the catalytic Rossmann-fold domain. The glutamylation ability of tRNA(Gln) by ND-GluRS was measured in the presence of the bacterial Glu-tRNA(Gln) amidotransferase GatCAB. Interestingly, the glutamylation efficiency was not affected even in the presence of excess GatCAB. Therefore, GluRS avoids competition with GatCAB and glutamylates tRNA(Gln).

PubMed: 20606262
DOI: 10.1107/S0907444910019086

Experimental method

X-RAY DIFFRACTION (2 Å)