3NCH
Yeast Glycogen Synthase (Gsy2p) Basal State Conformation
Summary for 3NCH
| Entry DOI | 10.2210/pdb3nch/pdb |
| Related | 1RZU 2BIS 3NAZ 3NB0 |
| Descriptor | Glycogen [starch] synthase isoform 2, SULFATE ION (2 entities in total) |
| Functional Keywords | glycogen synthase, allosteric activation, glucose-6-phosphate, transferase |
| Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 329891.95 |
| Authors | Baskaran, S.,Hurley, T.D. (deposition date: 2010-06-04, release date: 2010-10-06, Last modification date: 2023-09-06) |
| Primary citation | Baskaran, S.,Roach, P.J.,Depaoli-Roach, A.A.,Hurley, T.D. Structural basis for glucose-6-phosphate activation of glycogen synthase. Proc.Natl.Acad.Sci.USA, 107:17563-17568, 2010 Cited by PubMed Abstract: Regulation of the storage of glycogen, one of the major energy reserves, is of utmost metabolic importance. In eukaryotes, this regulation is accomplished through glucose-6-phosphate levels and protein phosphorylation. Glycogen synthase homologs in bacteria and archaea lack regulation, while the eukaryotic enzymes are inhibited by protein kinase mediated phosphorylation and activated by protein phosphatases and glucose-6-phosphate binding. We determined the crystal structures corresponding to the basal activity state and glucose-6-phosphate activated state of yeast glycogen synthase-2. The enzyme is assembled into an unusual tetramer by an insertion unique to the eukaryotic enzymes, and this subunit interface is rearranged by the binding of glucose-6-phosphate, which frees the active site cleft and facilitates catalysis. Using both mutagenesis and intein-mediated phospho-peptide ligation experiments, we demonstrate that the enzyme's response to glucose-6-phosphate is controlled by Arg583 and Arg587, while four additional arginine residues present within the same regulatory helix regulate the response to phosphorylation. PubMed: 20876143DOI: 10.1073/pnas.1006340107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.88 Å) |
Structure validation
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