catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase
Tyrosinyl-tRNA synthetase (TyrRS)/Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. These enzymes attach Tyr or Trp, respectively, to the appropriate tRNA. These class I enzymes are homodimers, which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.
Structure:1I6M_A; Geobacillus stearothermophilus TrpRS bound to Tryptophanyl-5'AMP using 4.0 A contacts - View structure with Cn3D
Structure:1JIJ_A; Staphylococcus aureus TyrRS binds inhibitor SB-239629 ([2-amino-3-(4-hydroxy-phenyl)-propionylamino]-(1,3,4,5-tetrahydroxy-4-hydroxymethyl-piperidin-2-yl)-acetic acid), defined using 4.0 A contacts - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",