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
Search PMC articles PubMed articles NCBI proteins

Ferredoxin-fold anticodon binding domain
the crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with cognate tRNA^Phe
Identifiers
Symbol	FDX-ACB
Pfam	PF03147
InterPro	IPR005121
SCOP	1pys
SUPERFAMILY	1pys
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

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

ATP + L-phenylalanine + tRNA^Phe $\rightleftharpoons$ AMP + diphosphate + L-phenylalanyl-tRNA^Phe

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

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

• Stulberg MP (1967). "The isolation and properties of phenylalanyl ribonucleic acid synthetase from Escherichia coli B". J. Biol. Chem. 242 (5): 1060–4. PMID 5335910.

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