3O3C

Glycogen synthase basal state UDP complex

3O3C の概要

• エントリーDOI: 10.2210/pdb3o3c/pdb
• 関連するPDBエントリー: 1RZU 2BIS
• 分子名称: Glycogen [starch] synthase isoform 2, SULFATE ION, URIDINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: glycogen synthase, transferase
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 331124.34

構造登録者

Baskaran, S.,Hurley, T.D. (登録日: 2010-07-23, 公開日: 2010-10-06, 最終更新日: 2023-09-06)

主引用文献

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

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: 20876143
DOI: 10.1073/pnas.1006340107

実験手法

X-RAY DIFFRACTION (3.512 Å)