Literature summary for 2.7.7.9 extracted from

Thoden, J.B.; Holden, H.M.
The molecular architecture of glucose-1-phosphate uridylyltransferase (2007), Protein Sci., 16, 432-440.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
protein is a tetramer with 222 point group symmetry. Each subunit is dominated by an eight-stranded mixed beta-sheet with two additional layers of beta-sheets and ten alpha-helices. Q109 and D137 anchor the uracil ring and the ribose of UDP-glucose to the protein.The beta-phosphoryl group of the product lies close to the epsilon-nitrogen of K202, the carboxylate group of E201 can bridge the 2- and 3-hydroxyl groups of the glucosyl moiety	Escherichia coli
to 1.9 A resolution. Modeling of UDP-glucose into the active site. The side chains of Gln109 and Asp137, respectively, serve to anchor the uracil ring and the ribose of UDP-glucose to the protein. The beta-phosphoryl group of the product is predicted to lie within hydrogen bonding distance to the eosilon-nitrogen of Lys202 whereas the carboxylate group of Glu201 is predicted to bridge the 2'- and 3'-hydroxyl groups of the glucosyl moiety	Escherichia coli

Crystallization (Comment)

Organism

protein is a tetramer with 222 point group symmetry. Each subunit is dominated by an eight-stranded mixed beta-sheet with two additional layers of beta-sheets and ten alpha-helices. Q109 and D137 anchor the uracil ring and the ribose of UDP-glucose to the protein.The beta-phosphoryl group of the product lies close to the epsilon-nitrogen of K202, the carboxylate group of E201 can bridge the 2- and 3-hydroxyl groups of the glucosyl moiety

Escherichia coli

to 1.9 A resolution. Modeling of UDP-glucose into the active site. The side chains of Gln109 and Asp137, respectively, serve to anchor the uracil ring and the ribose of UDP-glucose to the protein. The beta-phosphoryl group of the product is predicted to lie within hydrogen bonding distance to the eosilon-nitrogen of Lys202 whereas the carboxylate group of Glu201 is predicted to bridge the 2'- and 3'-hydroxyl groups of the glucosyl moiety

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AEP3	-	-

Subunits

Subunits	Comment	Organism
tetramer	crystallization data	Escherichia coli

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Release 2023.1 (January 2023)