3FGU

Catalytic complex of Human Glucokinase

3FGU の概要

• エントリーDOI: 10.2210/pdb3fgu/pdb
• 関連するPDBエントリー: 1V4S 1V4T 3F9M
• 分子名称: Glucokinase, beta-D-glucopyranose, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (6 entities in total)
• 機能のキーワード: glucokinase, hexokinase iv, atp-binding, diabetes mellitus, disease mutation, glycolysis, kinase, nucleotide-binding, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53745.94

構造登録者

Petit, P.,Lagarde, A.,Boutin, J.A.,Ferry, G.,Vuillard, L. (登録日: 2008-12-08, 公開日: 2009-12-15, 最終更新日: 2023-11-01)

主引用文献

Petit, P.,Antoine, M.,Ferry, G.,Boutin, J.A.,Lagarde, A.,Gluais, L.,Vincentelli, R.,Vuillard, L.
The active conformation of human glucokinase is not altered by allosteric activators
Acta Crystallogr.,Sect.D, 67:929-935, 2011

PubMed Abstract: Glucokinase (GK) catalyses the formation of glucose 6-phosphate from glucose and ATP. A specific feature of GK amongst hexokinases is that it can cycle between active and inactive conformations as a function of glucose concentration, resulting in a unique positive kinetic cooperativity with glucose, which turns GK into a unique key sensor of glucose metabolism, notably in the pancreas. GK is a target of antidiabetic drugs aimed at the activation of GK activity, leading to insulin secretion. Here, the first structures of a GK-glucose complex without activator, of GK-glucose-AMP-PNP and of GK-glucose-AMP-PNP with a bound activator are reported. All these structures are extremely similar, thus demonstrating that binding of GK activators does not result in conformational changes of the active protein but in stabilization of the active form of GK.

PubMed: 22101819
DOI: 10.1107/S0907444911036729

実験手法

X-RAY DIFFRACTION (2.15 Å)