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2.4.1.11: glycogen(starch) synthase

This is an abbreviated version!
For detailed information about glycogen(starch) synthase, go to the full flat file.

Word Map on EC 2.4.1.11

Reaction

UDP-alpha-D-glucose
+
[(1->4)-alpha-D-glucosyl]n
=
UDP
 +
[(1->4)-alpha-D-glucosyl]n+1

Synonyms

Cg-GYS, GBSS, GBSSI, glucosyltransferase, uridine diphosphoglucose-glycogen, glycogen synthase, glycogen synthase 2, glycogen synthase-2, glycogen synthetase (starch), granule bound starch synthase, granule-bound starch synthase, GS-I, GSN, GSY2p, Gys-2, GYS1, GYS2, Gys2p, starch synthase I, starch/glycogen synthase, TVAG_258220, UDP-glucose-glycogen glucosyltransferase, UDP-glycogen synthase, UDPG-glycogen synthetase, UDPG-glycogen transglucosylase, uridine diphosphoglucose-glycogen glucosyltransferase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.11 glycogen(starch) synthase

Crystallization

Crystallization on EC 2.4.1.11 - glycogen(starch) synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain bound to ADP and inhibitor acarbose, hanging drop vapor diffusion method, using 40 mM citric acid, 60 mM Bis-Tris propane, pH 6.4 and 20% (w/v) PEG 3350
crystals from the protein and from its selenomethionyl variant are grown in 100 mM sodium citrate pH 5.6 containing 20% PEG and 20% dioxane by hanging drop vapour-diffusion method at 20°C. Crystals grow in thin needles, diffract to 3.5 A resolution and belong to space group C2, with unit-cell parameters a = 202 A, b = 73 A, c = 149 A, beta = 131°
-
purified recombinant enzyme in complex with UDP-Glc, sitting drop vapor diffusion method, 0.002 ml of 5 mg/ml protein in 50-mM Tris-HCl, pH 7.4, with 10 mM UDP-Glc is mixed with 0.002 ml reservoir solution containing 0.1-M sodium citrate, pH 4.0, and 20-28% 2-methyl-2,4-pentanediol, 2 months, 20°C, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement
-
sitting drop vapor diffusion method
-
purified recombinant His-tagged enzyme, basal state and glucose-6-phosphate activated state Gsy2p, X-ray diffraction structure determination and analysis at 3.0 A and 2.4 A, respectively, modeling
-