InterPro domain: IPR023509

D-tyrosyl-tRNA(Tyr) deacylase (DTD), also known as D-aminoacyl-tRNA deacylase, is an editing enzyme that removes D-amino acids from mischarged tRNAs. Structural studies have shown various different modes of D-amino acid recognition by DTDs, suggesting an inherent plasticity that can accommodate all d-amino acids. DTDs are essentially inactive toward L-aa-tRNAs [ 1 , 2 ].

This superfamily represents a DTD fold, consisting of a beta-barrel closed on one side by a beta-sheet lid [ 3 ]. The DTD fold is present across the domains of life in twodifferent functional contexts: as an N-terminal editing domain of archaeal ThrRS (Threonyl-tRNA synthetase), which specifically removes noncognateL-serine mischarged on tRNAThr, and as a freestanding'chiral proofreading' enzyme, which removes D-amino acids fromtRNAs in bacteria and eukaryotes [ 4 ].

1. Ligand-bound structures provide atomic snapshots for the catalytic mechanism of D-amino acid deacylase. J. Biol. Chem. 285, 5917-30
2. Structure of D-tyrosyl-tRNATyr deacylase using home-source Cu Kalpha and moderate-quality iodide-SAD data: structural polymorphism and HEPES-bound enzyme states. Acta Crystallogr D Biol Crystallogr 66, 584-92
3. Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases. J. Biol. Chem. 276, 47285-90
4. Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme. Nat Commun 6, 7552