Literature summary for 6.1.1.20 extracted from

Moor, N.; Kotik-Kogan, O.; Tworowski, D.; Sukhanova, M.; Safro, M.
The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end (2006), Biochemistry, 45, 10572-10583.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Thermus thermophilus

Crystallization (Comment)

Organism

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

Thermus thermophilus

Inhibitors

Inhibitors	Comment	Organism	Structure
PheOH-AMP	L-phenylalaninyl-5'-adenylate, a nonhydrolyzable phenylalanyladenylate analogue, conformational changes in tRNAPhe and the catalytic domain are induced by the PheOH-AMP binding: the motif 2 loop and a helical loop, residues 139-152 of the alpha-subunit, undergo coordinated displacement, Metalpha148 of the helical loop adopts a conformation preventing the 2'-OH group of A76 from approaching the alpha-carbonyl carbon of PheOH-AMP, the unfavorable position of the terminal ribose stems from the absence of the R-carbonyl oxygen in the analogue, overview	Thermus thermophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-phenylalanine + tRNAPhe	Thermus thermophilus	-	AMP + diphosphate + L-phenylalanyl-tRNAPhe	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + L-phenylalanine + tRNAPhe	-	Thermus thermophilus	AMP + diphosphate + L-phenylalanyl-tRNAPhe	-	?
ATP + L-phenylalanine + tRNAPhe	charging of cognate amino acid, conformational changes in tRNAPhe and the catalytic domain are induced by the PheOH-AMP or AMP binding, acceptor arm binding and recognition	Thermus thermophilus	AMP + diphosphate + L-phenylalanyl-tRNAPhe	-	?
additional information	tRNAPhe binding structure determination: CCA end orientation is stabilized by extensive base-specific interactions of A76 and C75 with the protein and by intra-RNA interactions of A73 with adjacent nucleotides, the 4-amino group of the bulged out C75 is trapped by two negatively charged residues of the beta-subunit, Glubeta31 and Aspbeta33, highly conserved in eubacterial PheRSs, the position of the A76 base is stabilized by interactions with HisR212 of motif 2 (universally conserved in PheRSs) and class II-invariant ArgR321 of motif 3, overview	Thermus thermophilus	?	-	?

Subunits

Subunits	Comment	Organism
tetramer	(alphabeta)2 heterotetramer	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
Phenylalanyl-tRNA synthetase	-	Thermus thermophilus
PheRS	-	Thermus thermophilus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Thermus thermophilus