Literature summary for 2.4.1.21 extracted from

Sheng, F.; Yep, A.; Feng, L.; Preiss, J.; Geiger, J.H.
Oligosaccharide binding in Escherichia coli glycogen synthase (2009), Biochemistry, 48, 10089-10097.

Crystallization (Commentary)

Crystallization (Comment)	Organism
cocrystallization of the inactive glycogen synthase mutant E377A with substrate ADPGlc and cocrystallization of wild-type glycogen synthase with substrate ADPGlc and the glucan acceptor mimic 4-(2-hydroxyethyl)piperazine-1-(2-hydroxypropane)sulfonic acid, i.e. HEPPSO produces a closed form of glycogen synthase and suggests that domain-domain closure accompanies glycogen synthesis. Four bound oligosaccharides are observed, G6a in the interdomain cleft and G6b, G6c, and G6d on the N-terminal domain surface. Extending from the center of the enzyme to the interdomain cleft opening, G6a mostly interacts with the highly conserved N-terminal domain residues lining the cleft of glycogen synthase. The surface-bound oligosaccharides G6c and G6d have less interaction with enzyme and exhibit a more curled, helixlike structural arrangement	Escherichia coli

Crystallization (Comment)

Organism

cocrystallization of the inactive glycogen synthase mutant E377A with substrate ADPGlc and cocrystallization of wild-type glycogen synthase with substrate ADPGlc and the glucan acceptor mimic 4-(2-hydroxyethyl)piperazine-1-(2-hydroxypropane)sulfonic acid, i.e. HEPPSO produces a closed form of glycogen synthase and suggests that domain-domain closure accompanies glycogen synthesis. Four bound oligosaccharides are observed, G6a in the interdomain cleft and G6b, G6c, and G6d on the N-terminal domain surface. Extending from the center of the enzyme to the interdomain cleft opening, G6a mostly interacts with the highly conserved N-terminal domain residues lining the cleft of glycogen synthase. The surface-bound oligosaccharides G6c and G6d have less interaction with enzyme and exhibit a more curled, helixlike structural arrangement

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
E377A	inactive, crystallization data	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6U8	-	-

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Release 2023.1 (January 2023)