InterPro domain: IPR005121

Aminoacyl-tRNA synthetases (aaRSs) play a crucial role in the translation of the genetic code by means of covalent attachment of amino acids to theircognate tRNAs. Phenylalanine-tRNA synthetase (PheRS, also known as Phenylalanine-tRNA ligase) is known to be among themost complex enzymes of the aaRS family. Bacterial and mitochondrial PheRSsshare a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents acanonical double split alpha+beta motif having no insertions. The FDX-ACBdomain displays a typical RNA recognition fold (RRM) (see PDOC00030 ) formed by the four-stranded antiparallel beta sheet, with two helices packed against it [ 1 , 2 , 3 , 4 , 5 ].

1. Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus. Nat. Struct. Biol. 2, 537-47
2. The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe. Structure 5, 59-68
3. Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells. Biochem. Biophys. Res. Commun. 255, 765-73
4. Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end. Biochemistry 42, 10697-708
5. The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase. Structure 16, 1095-104