3QIC

The structure of human glucokinase E339K mutation

3QIC の概要

• エントリーDOI: 10.2210/pdb3qic/pdb
• 関連するPDBエントリー: 1V4S 3F9M 3ID8
• 分子名称: Glucokinase, alpha-D-glucopyranose, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: glycolysis, kinase, sugar binding, phosphorylation, 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: 53808.95

構造登録者

Liu, Q.,Liu, S.,Liu, J. (登録日: 2011-01-27, 公開日: 2011-06-01, 最終更新日: 2024-10-30)

主引用文献

Liu, Q.,Shen, Y.,Liu, S.,Weng, J.,Liu, J.
Crystal structure of E339K mutated human glucokinase reveals changes in the ATP binding site.
Febs Lett., 585:1175-1179, 2011

PubMed Abstract: Human glucokinase (GK) plays an important role in glucose homeostasis. An E339K mutation in GK was recently found to be associated with hyperglycemia. It showed lower enzyme activity and impaired protein stability compared to the wild-type enzyme. Here, we present the crystal structure of E339K GK in complex with glucose. This mutation results in a conformational change of His416, spatially interfering with adenosine-triphosphate (ATP) binding. Furthermore, Ser411 at the ATP binding site is phosphorylated and then hydrogen bonded with Thr82, physically blocking the ATP binding. These findings provide structural basis for the reduced activity of this mutant.

PubMed: 21420961
DOI: 10.1016/j.febslet.2011.03.026

実験手法

X-RAY DIFFRACTION (2.2 Å)