Literature summary for 6.1.1.2 extracted from

Arakaki, T.L.; Carter, M.; Napuli, A.J.; Verlinde, C.L.; Fan, E.; Zucker, F.; Buckner, F.S.; Van Voorhis, W.C.; Hol, W.G.; Merritt, E.A.
The structure of tryptophanyl-tRNA synthetase from Giardia lamblia reveals divergence from eukaryotic homologs (2010), J. Struct. Biol., 171, 238-243.

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified TrpRS, grown at room temperature by vapor equilibration from sitting drops containing 0.002 ml of protein solution containing 11 mg/ml protein, 500 mM NaCl, 20 mM HEPES, 2 mM BME, 5% glycerol, 0.025% NaAzide, pH 7.5, mixed with 0.001 ml of crystallization buffer containing 2.7 M ammonium sulfate, 5 mM DTT, 0.1 M citric acid, pH 5.2, X-ray diffraction structure determination and analysis at 2.1 A resolution	Giardia intestinalis

Crystallization (Comment)

Organism

purified TrpRS, grown at room temperature by vapor equilibration from sitting drops containing 0.002 ml of protein solution containing 11 mg/ml protein, 500 mM NaCl, 20 mM HEPES, 2 mM BME, 5% glycerol, 0.025% NaAzide, pH 7.5, mixed with 0.001 ml of crystallization buffer containing 2.7 M ammonium sulfate, 5 mM DTT, 0.1 M citric acid, pH 5.2, X-ray diffraction structure determination and analysis at 2.1 A resolution

Giardia intestinalis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Giardia intestinalis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-tryptophan + tRNATrp	Giardia intestinalis	-	AMP + diphosphate + L-tryptophyl-tRNATrp	-	?

Organism

Organism	UniProt	Comment	Textmining
Giardia intestinalis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + L-tryptophan + tRNATrp	-	Giardia intestinalis	AMP + diphosphate + L-tryptophyl-tRNATrp	-	?
ATP + L-tryptophan + tRNATrp	the active site is located in a deep, long pocket within the catalytic domain, and is surrounded by several conserved features	Giardia intestinalis	AMP + diphosphate + L-tryptophyl-tRNATrp	-	?
additional information	modeling of probable tRNA binding, overview	Giardia intestinalis	?	-	?

Subunits

Subunits	Comment	Organism
tetramer	(alpha2)2 homotetramer, crystal structure analysis, the N-terminus forms a 16-residue a-helix, structure modelling, overview. The typical class I aminoacyl-tRNA synthetase contains an N-terminal extension, residues 1-64, a Rossman-fold catalytic domain, residues 65-324, 415-429, and an anticodon recognition domain, residues 325-414	Giardia intestinalis

Synonyms

Synonyms	Comment	Organism
More	the enzyme belongs to the class I aminoacyl-tRNA synthetases	Giardia intestinalis
TrpRS	-	Giardia intestinalis
Tryptophanyl-tRNA synthetase	-	Giardia intestinalis

Cofactor

Cofactor	Comment	Organism	Structure
ATP	the ATP-binding site, a loop formed by the residues 311-315 of the KMSAS motif, is sandwiched by the characteristic class I HIGH motif, residues 84-87, and by residues 272-275 of a GIEQ motif that is weakly conserved among TrpRS sequences	Giardia intestinalis

General Information

General Information	Comment	Organism
evolution	the activation reaction mechanism of TrpRS from the basal eukaryote Gardia lamblia differs from that of higher eukaryotes, overview. The N-terminus of the class I aminoacyl-tRNA synthetase from Gardia lamblia forms a 16-residue alpha-helix. This helix replaces a beta-hairpin that is required by human TrpRS for normal activity and infers to play a similar role in all eukaryotic TrpRS	Giardia intestinalis