Phenylalanine—tRNA ligase

phenylalanine-tRNA ligase
Identifiers
EC number 6.1.1.20
CAS number 9055-66-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Ferredoxin-fold anticodon binding domain

the crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with cognate tRNAPhe
Identifiers
Symbol FDX-ACB
Pfam PF03147
InterPro IPR005121
SCOP 1pys
SUPERFAMILY 1pys

In enzymology, a phenylalanine-tRNA ligase (EC 6.1.1.20) is an enzyme that catalyzes the chemical reaction

ATP + L-phenylalanine + tRNAPhe \rightleftharpoons AMP + diphosphate + L-phenylalanyl-tRNAPhe

The 3 substrates of this enzyme are ATP, L-phenylalanine, and tRNAPhe, whereas its 3 products are AMP, diphosphate, and L-phenylalanyl-tRNAPhe.

This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-phenylalanine:tRNAPhe ligase (AMP-forming). Other names in common use include phenylalanyl-tRNA synthetase, phenylalanyl-transfer ribonucleate synthetase, phenylalanine-tRNA synthetase, phenylalanyl-transfer RNA synthetase, phenylalanyl-tRNA ligase, phenylalanyl-transfer RNA ligase, L-phenylalanyl-tRNA synthetase, and phenylalanine translase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyl-tRNA biosynthesis.

Phenylalanine-tRNA synthetase (PheRS) is known to be among the most complex enzymes of the aaRS (Aminoacyl-tRNA synthetase) family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split alpha+beta motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold (RRM) formed by the four-stranded antiparallel beta sheet, with two helices packed against it.[1][2][3][4][5]

Structural studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1B70, 1B7Y, 1EIY, 1JJC, 1PYS, 2AKW, 2ALY, 2AMC, 2CXI, and 2IY5.

References

  1. ↑ Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG (July 1995). "Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus". Nat. Struct. Biol. 2 (7): 537–47. doi:10.1038/nsb0795-537. PMID 7664121.
  2. ↑ Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M (January 1997). "The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe". Structure 5 (1): 59–68. doi:10.1016/s0969-2126(97)00166-4. PMID 9016717.
  3. ↑ Rodova M, Ankilova V, Safro MG (February 1999). "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 (3): 765–73. doi:10.1006/bbrc.1999.0141. PMID 10049785.
  4. ↑ Moor N, Lavrik O, Favre A, Safro M (September 2003). "Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end". Biochemistry 42 (36): 10697–708. doi:10.1021/bi034732q. PMID 12962494.
  5. ↑ Klipcan L, Levin I, Kessler N, Moor N, Finarov I, Safro M (July 2008). "The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase". Structure 16 (7): 1095–104. doi:10.1016/j.str.2008.03.020. PMID 18611382.

Further reading

    This article incorporates text from the public domain Pfam and InterPro IPR005121

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