EC Number   |
|---|
    2.4.1.21 | catalytic domain bound to ADP and inhibitor acarbose, hanging drop vapor diffusion method, using 0.2 MLi2SO4, 0.1MBis-Tris pH 5.5, 25% (w/v) PEG3350 |
| 2.4.1.21 | catalytic domain bound to ADP and inhibitor acarbose, hanging drop vapor diffusion method, using 2 M (NH4)2SO4, 2% (w/v) PEG400 and 150 mM HEPES pH 7.5 |
| 2.4.1.21 | 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 |
| 2.4.1.21 | sitting drop vapor diffusion method, using 100 mM sodium cacodylate buffer pH 6.5, 17% (w/v)v PEG 8K, 0.2 M ammonium sulfate |
| 2.4.1.21 | structure of the wild-type enzyme bound to ADP and glucose reveals a 15.2° overall domain-domain closure. The main chain carbonyl group of His-161, Arg-300, and Lys-305 are suggested to act as critical catalytic residues in the transglycosylation. Glu-377 is found on the-face of the glucose and plays an electrostatic role in the active site and as a glucose ring locator. In the mutant E377A-ADP-4-(2-hydroxyethyl)piperazine-1-(2-hydroxypropane)sulfonic acid complex the glucose moiety is either absent or disordered in the active site |
