Literature summary for 3.6.5.3 extracted from

Knudsen, C.; Wieden, H.J.; Rodnina, M.V.
The importance of structural transitions of the switch II region for the functions of elongation factor Tu on the ribosome (2001), J. Biol. Chem., 276, 22183-22190.

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Protein Variants

Protein Variants	Comment	Organism
G83A	mutation slows down the association of the ternary complex EF-Tu/GTP/aminoacyltRNA with the ribosome and abolishes the ribosome-induced GTPase activity of EF-Tu	Escherichia coli
G83A/G94A	mutation slows down the association of the ternary complex EF-Tu/GTP/aminoacyltRNA with the ribosome and abolishes the ribosome-induced GTPase activity of EF-Tu	Escherichia coli
G94A	mutation strongly impairs the conformational change of EF-Tu from the GTP-bound to the GDP-bound form and decelerates the dissociation of EF-Tu/GDP from the ribosome	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + H2O	-	Escherichia coli	GDP + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
EF-Tu	-	Escherichia coli
elongation factor Tu	-	Escherichia coli

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Release 2023.1 (January 2023)