Literature summary for 6.1.1.2 extracted from

Yu, Y.; Liu, Y.; Shen, N.; Xu, X.; Xu, F.; Jia, J.; Jin, Y.; Arnold, E.; Ding, J.
Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity (2004), J. Biol. Chem., 279, 8378-8388.

Crystallization (Commentary)

Crystallization (Comment)	Organism
catalytic fragment, hanging drop method, 0.002 ml protein solution: 8 mg/ml protein, 20 mM Tris-potassium phosphate, pH 6.8, 10 mM MgCl2, 5 mM 2-mercaptoethanol, plus equal volume of reservoir solution: 16% w/v polyethylene glycol 1500, 4% polyehylene glycol 3350, 0.2 M trisodium citrate dihydrate, pH 8.2, plus 0.0005 ml 30% 2-methyl-2,4-pentanediol, 7-10 days, 4°C, proteolytic cleavage of the enzyme into 2 fragments occurs during the crystallization process, X-ray diffraction structure determination at 2.5 A resolution using the MAD method, and analysis	Homo sapiens

Crystallization (Comment)

Organism

catalytic fragment, hanging drop method, 0.002 ml protein solution: 8 mg/ml protein, 20 mM Tris-potassium phosphate, pH 6.8, 10 mM MgCl2, 5 mM 2-mercaptoethanol, plus equal volume of reservoir solution: 16% w/v polyethylene glycol 1500, 4% polyehylene glycol 3350, 0.2 M trisodium citrate dihydrate, pH 8.2, plus 0.0005 ml 30% 2-methyl-2,4-pentanediol, 7-10 days, 4°C, proteolytic cleavage of the enzyme into 2 fragments occurs during the crystallization process, X-ray diffraction structure determination at 2.5 A resolution using the MAD method, and analysis

Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-tryptophan + tRNATrp	Homo sapiens	-	AMP + diphosphate + L-tryptophan-tRNATrp	-	?
additional information	Homo sapiens	the catalytic fragment exhibits potent angiostatic activity	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P23381	recombinant purified native and selenomethionyl-enzyme	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	a full-length and 3 N-terminal truncated enzyme forms by alternative splicing and proteolytic cleavage, the shortest fragment comprises the catalytic activity	Homo sapiens

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp	wide opening active site that adopts a compact conformation, modeling of substrate recognition and binding	Homo sapiens	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-tryptophan + tRNATrp	-	Homo sapiens	AMP + diphosphate + L-tryptophan-tRNATrp	-	?
additional information	the catalytic fragment exhibits potent angiostatic activity	Homo sapiens	?	-	?

Synonyms

Synonyms	Comment	Organism
TrpRS	-	Homo sapiens
Tryptophanyl-tRNA synthase	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Homo sapiens