Literature summary for 6.1.1.2 extracted from

Shen, N.; Zhou, M.; Yang, B.; Yu, Y.; Dong, X.; Ding, J.
Catalytic mechanism of the tryptophan activation reaction revealed by crystal structures of human tryptophanyl-tRNA synthetase in different enzymatic states (2008), Nucleic Acids Res., 36, 1288-1299.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of hTrpRS in complexes with Trp, tryptophanamide and ATP and tryptophanyl-AMP, respectively, are all determined at 2.4 A resolution	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P23381	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp	recognition of Trp is by an induced-fit mechanism involving conformational change of the AIDQ motif that creates a perfect pocket for the binding and activation of Trp and causes coupled movements of the N-terminal and C-terminal domains. The KMSAS loop has an inherent flexibility and binding of ATP stabilizes it in a closed conformation that secures the position of ATP for catalysis. Structural data indicate that the catalytic mechanism of the Trp activation reaction by hTrpRS involves more moderate conformational changes of the structural elements at the active site compared to bacterial TrpRS	Homo sapiens	a

Subunits

Subunits	Comment	Organism
dimer	method: crystal structure. Dimeric hTrpRS is structurally and functionally asymmetric with half of-the-sites reactivity	Homo sapiens

Synonyms

Synonyms	Comment	Organism
hTrpRS	-	Homo sapiens
trytophanyl-tRNA synthetase	-	Homo sapiens

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Release 2023.1 (January 2023)