Literature summary for 6.1.1.20 extracted from

Mermershtain, I.; Finarov, I.; Klipcan, L.; Kessler, N.; Rozenberg, H.; Safro, M.G.
Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP (2011), Protein Sci., 20, 160-167.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of His-tagged PheRs in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Escherichia coli

Crystallization (Comment)

Organism

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

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P08312	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged PheRs from Escherichia coli	Escherichia coli

Subunits

Subunits	Comment	Organism
heterotetramer	EcPheRS is a (alphabeta)2 heterotetramer, built of two alphabeta heterodimers	Escherichia coli
More	EcPheRS consists of 11 structural domains. Three of them: the N-terminus, A1 and A2 belong to the alpha-subunit and B1-B8 domains to the beta subunit. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain, structure comparisons, overview	Escherichia coli

Synonyms

Synonyms	Comment	Organism
More	the enzyme belongs to class II aminoacyl-tRNA synthetases	Escherichia coli
Phenylalanyl-tRNA synthetase	-	Escherichia coli
PheRS	-	Escherichia coli

General Information

General Information	Comment	Organism
evolution	architecture of four helix-bundle interface, characteristic of class IIc heterotetrameric aaRSs, is changed, each of the two long helices belonging to CLM transformed into the coil-short helix structural fragments. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain	Escherichia coli