Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.1.1.20: phenylalanine-tRNA ligase

This is an abbreviated version!
For detailed information about phenylalanine-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.20

Reaction

ATP
+
L-phenylalanine
 +
tRNAPhe
=
AMP
 +
diphosphate
 +
L-phenylalanyl-tRNAPhe

Synonyms

CML33, ctPheRS, cytoplasmic phenylalanyl-tRNA synthetase, cytosolic phenylalanyl-tRNA synthetase, cytosolic PheRS, EcPheRS, FARS2, FRS, hcPheRS, HSPC173, L-Phenylalanyl-tRNA synthetase, mitochondrial phenylalanyl-tRNA synthetase, mitochondrial PheRS, mitPheRS, More, mtPheRS, p-azido-phenylalanyl-tRNA synthetase, pAzFRS, Phe-RS, Phenylalanine translase, phenylalanine tRNA synthetase, Phenylalanine--tRNA ligase, Phenylalanine-tRNA synthetase, Phenylalanyl transfer ribonucleic acid synthetase, Phenylalanyl-transfer ribonucleate synthetase, Phenylalanyl-transfer RNA ligase, Phenylalanyl-transfer RNA synthetase, Phenylalanyl-tRNA ligase, Phenylalanyl-tRNA synthetase, PheRS, PheRS-alpha, Synthetase, phenylalanyl-transfer ribonucleate

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.20 phenylalanine-tRNA ligase

Crystallization

Crystallization on EC 6.1.1.20 - phenylalanine-tRNA ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and SeMet-labeled PheRs in complex with phenylalanine and AMP, hanging-drop vapor-diffusion method, 20°C using 0.004 ml of protein solution, containing 10 mg/ml protein and 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 1 mM EDTA, 1 mM MgCl2, 10% glycerol, 1 mM Phe and 1 mM ATP, are mixed at 1:1 ratio with precipitant containing 17-20% PEG 8000K, 0.2 M MgCl2, 0.1 M Tris-HCl buffer, pH 8.5, 3% 1,6 hexandiol, and 3% D-galactose, 3 days, mother-liquor solution containing 20% v/v ethylene-glycol, X-ray diffraction structure determination and analysis at 3.05 A resolution
in complex with 3,4-dihydroxy-L-phenylalanine
purified mitochondrial PheRS complexed with Phe-AMP, cryoprotection by mother liquor solution containing 25% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
purified recombinant mitPheRS in complex with L-phenylalanine and ATP, hanging or sitting drop vapour diffusion method, 0.001-0.003 ml of protein solution containing 6 mg/ml protein in 20 mM Tris-HCl pH 8.0, 100 mM NaCl, 7 mM MgCl2, 5 mM 2-mercaptoethanol, 1 mM EDTA and 0.0065% NaN3, is mixed with an equal volume of reservoir solution containing 25 mM Tris-HCl pH 8.5, 10 mM MgCl2, 5 mM ATP, 2 mM L-phenylalanine, equilibration against reservoir solution, at 4°C or 19°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
the structure of cytosolic phenylalanyl-tRNA synthetase in complex with phenylalanine is solved to 3.3 A resolution
the structure of human cytoplasmic phenylalanyl-tRNA synthetase is determined to a resolution of 3.3 A
purified recombinant selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit, 0.001 ml of protein solution containing 36 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 200 mM NaCl, mixed with 0.001 ml of precipitant solution, containing 100 mM sodium citrate, pH 5.6, and 16.5% PEG 20000, covarage with a 1:1 mixture of paraffin oil and silicone, 20°C, 1 week, soaking in a soaked in a cryoprotectant solution containing 100 mM sodium citrate, pH 5.6, 18.2% PEG 20000, and 20% glycerol, X-ray diffraction structure determination and analysis at 1.94 A resolution
native enzyme crystals are of poor quality diffracting only to 3-5 A resolution, engineered mutant enzymes diffracts to 2.0 A resolution, X-ray diffraction structure determination and analysis, overview
-
at 0.6-nm resolution
-
crystal structure at 2.9 A resolution
-
crystal structure of complexes of enzyme with L-Tyr, p-chlorophenylalanine, and L-tyrosyl-adenylate
-
crystal structure of enzyme complexed with cognate tRNAPhe
-
enzyme complexed with phenylalanine or the phenylalanyl-adenylate analogue phenylalaninyl-adenylate, X-ray diffraction structure determination at 2.7 and 2.5 A resolution, respectively, and analysis
-
in complex with 3,4-dihydroxy-L-phenylalanine
-
native enzyme complexed with phenylalanyl-adenylate in presence of manganese, X-ray diffraction structure determination at 2.6 A resolution and analysis
-
PheRS in complex with with cognate tRNAPhe and nonhydrolyzable phenylalanyladenylate analogue PheOH-AMP, hanging-drop vapor-diffusion method, 4°C, 3-5 mg/ml protein ina ratio of 1:2,5 with tRNAPhe in 20 mM imidazole-HCl, pH 7.8, 1 mM MgCl2, 5 mM 2-mercaptoethanol, 1 mM NaN3, 10% saturated ammonium sulfate, and 1 mM PheOH-AMP, slow equilibration against a reservoir solution containing the crystallization buffer and 27% saturated ammonium sulfate, cryoprotection by 30% v/v glycerol, X-ray diffraction structure determination and anaylsis at 3.1 A resolution, modeling
-