4Z5X

Glycogen phosphorylase in complex with gallic acid

4Z5X の概要

• エントリーDOI: 10.2210/pdb4z5x/pdb
• 関連するPDBエントリー: 4YUA
• 分子名称: Glycogen phosphorylase, muscle form, 3,4,5-trihydroxybenzoic acid, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: alpha and beta protein, transferase
• 由来する生物種: Oryctolagus cuniculus (Rabbit)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 97855.66

構造登録者

Kyriakis, E.,Kantsadi, L.A.,Stravodimos, A.G.,Chatzileontiadou, S.M.D.,Leonidas, D.D. (登録日: 2015-04-03, 公開日: 2015-05-13, 最終更新日: 2025-04-09)

主引用文献

Kyriakis, E.,Stravodimos, G.A.,Kantsadi, A.L.,Chatzileontiadou, D.S.,Skamnaki, V.T.,Leonidas, D.D.
Natural flavonoids as antidiabetic agents. The binding of gallic and ellagic acids to glycogen phosphorylase b.
Febs Lett., 589:1787-1794, 2015

PubMed Abstract: We present a study on the binding of gallic acid and its dimer ellagic acid to glycogen phosphorylase (GP). Ellagic acid is a potent inhibitor with Kis of 13.4 and 7.5 μM, in contrast to gallic acid which displays Kis of 1.7 and 3.9 mM for GPb and GPa, respectively. Both compounds are competitive inhibitors with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP. However, only ellagic acid functions with glucose in a strongly synergistic mode. The crystal structures of the GPb-gallic acid and GPb-ellagic acid complexes were determined at high resolution, revealing that both ligands bind to the inhibitor binding site of the enzyme and highlight the structural basis for the significant difference in their inhibitory potency.

PubMed: 25980608
DOI: 10.1016/j.febslet.2015.05.013

実験手法

X-RAY DIFFRACTION (2.1 Å)