Literature summary for 6.1.1.20 extracted from

Evdokimov, A.G.; Mekel, M.; Hutchings, K.; Narasimhan, L.; Holler, T.; McGrath, T.; Beattie, B.; Fauman, E.; Yan, C.; Heaslet, H.; Walter, R.; Finzel, B.; Ohren, J.; McConnell, P.; Braden, T.; Sun, F.; Spessard, C.; Banotai, C.; Al-Kassim, L.; Ma, W.; Wengender, P.; Kole, D.; Garceau, N.; Toogood, P.; Liu, J.
Rational protein engineering in action: The first crystal structure of a phenylalanine tRNA synthetase from Staphylococcus haemolyticus (2008), J. Struct. Biol., 162, 152-169.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes	Staphylococcus haemolyticus

Crystallization (Comment)	Organism
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	Staphylococcus haemolyticus

Protein Variants	Comment	Organism
additional information	construction of enzyme mutants with better crystallization abilities, e.g. a PheRS variant which has both domains I and IV removed, or PheRS surface mutants, overview	Staphylococcus haemolyticus

Inhibitors	Comment	Organism	Structure
1-[3-[(4-pyridin-2-ylpiperazin-1-yl)sulfonyl]phenyl]-3-(1,3-thiazol-2-yl)urea	binding structure and inhibition mechanism, the inhibitor molecule binds with ring A deep inside the enzyme, and ring B in the place that is occupied by the aromatic ring of phenylalanine, overview	Staphylococcus haemolyticus

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Staphylococcus haemolyticus
additional information	enzyme metal binding site structure, overview	Staphylococcus haemolyticus

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

Organism	UniProt	Comment	Textmining
Staphylococcus haemolyticus	-	-	-

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-phenylalanine + tRNAPhe	-	Staphylococcus haemolyticus	AMP + diphosphate + L-phenylalanyl-tRNAPhe	-	?
ATP + L-phenylalanine + tRNAPhe	structure-activity relationship, overview	Staphylococcus haemolyticus	AMP + diphosphate + L-phenylalanyl-tRNAPhe	-	?

Subunits	Comment	Organism
More	structure analysis and structure-activity relationship, overview	Staphylococcus haemolyticus

Synonyms	Comment	Organism
phenylalanine tRNA synthetase	-	Staphylococcus haemolyticus
PheRS	-	Staphylococcus haemolyticus

Cofactor	Comment	Organism	Structure
ATP	-	Staphylococcus haemolyticus