Literature summary for 2.3.2.6 extracted from

Dong, X.; Kato-Murayama, M.; Muramatsu, T.; Mori, H.; Shirouzu, M.; Bessho, Y.; Yokoyama, S.
The crystal structure of leucyl/phenylalanyl-tRNA-protein transferase from Escherichia coli (2007), Protein Sci., 16, 528-534.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
1.6 A resolution crystal structure	Escherichia coli
enzyme adopts a monomeric structure consisting of two domains that form a bilobate molecule. The n-terminal domain forms a small lobe with an unusual fold. The large C-terminal domain has a highly conserved fold. Comparison with bacterial peptidoglycan synthase FemX	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Escherichia coli	P0A8P1	-	-

Synonyms

Synonyms	Comment	Organism
L/F-transferase	-	Escherichia coli
leucyl/phenylalanyl-tRNA-protein transferase	-	Escherichia coli

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Release 2023.1 (January 2023)