2ZJ4

Isomerase domain of human glucose:fructose-6-phosphate amidotransferase

2ZJ4 の概要

• エントリーDOI: 10.2210/pdb2zj4/pdb
• 関連するPDBエントリー: 2ZJ3
• 分子名称: Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1, 2-DEOXY-2-AMINO GLUCITOL-6-PHOSPHATE (3 entities in total)
• 機能のキーワード: glucosamine-6-phosphate synthase, aldose/ketose isomerase, rossmann-like fold, transferase, alternative splicing, aminotransferase, glutamine amidotransferase, phosphoprotein
• 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: 42580.30

構造登録者

Nakaishi, Y.,Bando, M.,Kondo, K.,Tsuge, H. (登録日: 2008-02-29, 公開日: 2009-01-13, 最終更新日: 2023-11-01)

主引用文献

Nakaishi, Y.,Bando, M.,Shimizu, H.,Watanabe, K.,Goto, F.,Tsuge, H.,Kondo, K.,Komatsu, M.
Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes
Febs Lett., 583:163-167, 2009

PubMed Abstract: Glutamine:fructose-6-phosphate amidotransferase (GFAT) is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes. We now report the first structures of the isomerase domain of the human GFAT in the presence of cyclic glucose-6-phosphate and linear glucosamine-6-phosphate. The C-terminal tail including the active site displays a rigid conformation, similar to the corresponding Escherichia coli enzyme. The diversity of the CF helix near the active site suggests the helix is a major target for drug design. Our study provides insights into the development of therapeutic drugs for type 2 diabetes.

PubMed: 19059404
DOI: 10.1016/j.febslet.2008.11.041

実験手法

X-RAY DIFFRACTION (2.2 Å)