Literature summary for 2.7.7.9 extracted from

McCoy, J.G.; Bitto, E.; Bingman, C.A.; Wesenberg, G.E.; Bannen, R.M.; Kondrashov, D.A.; Phillips, G.N.
Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP (2007), J. Mol. Biol., 366, 830-841.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
uncomplexed enzyme and in presence of UTP and UDP-glucose. Structures show a carboxy-terminal beta-helix domain in a unique orientation. The nucleotide binding loop and the carboxy-terminal domain, including the possible catalytically important K360, move in and out of the active site in a concerted fashion	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9M9P3	-	-

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Release 2023.1 (January 2023)