3R2W

Crystal Structure of UDP-glucose Pyrophosphorylase of Homo Sapiens

3R2W の概要

• エントリーDOI: 10.2210/pdb3r2w/pdb
• 分子名称: UTP--glucose-1-phosphate uridylyltransferase (1 entity in total)
• 機能のキーワード: homo sapiens, rossmann fold beta barrel, nucleotidyltransferase, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 236737.61

構造登録者

Zheng, X.,Yu, Q. (登録日: 2011-03-14, 公開日: 2012-02-08, 最終更新日: 2024-02-21)

主引用文献

Yu, Q.,Zheng, X.
The crystal structure of human UDP-glucose pyrophosphorylase reveals a latch effect that influences enzymatic activity.
Biochem.J., 442:283-291, 2012

PubMed Abstract: UGPase (UDP-glucose pyrophosphorylase) is highly conserved among eukaryotes. UGPase reversibly catalyses the formation of UDP-glucose and is critical in carbohydrate metabolism. Previous studies have mainly focused on the UGPases from plants, fungi and parasites, and indicate that the regulatory mechanisms responsible for the enzyme activity vary among different organisms. In the present study, the crystal structure of hUGPase (human UGPase) was determined and shown to form octamers through end-to-end and side-by-side interactions. The observed latch loop in hUGPase differs distinctly from yUGPase (yeast UGPase), which could explain why hUGPase and yUGPase possess different enzymatic activities. Mutagenesis studies showed that both dissociation of octamers and mutations of the latch loop can significantly affect the UGPase activity. Moreover, this latch effect is also evolutionarily meaningful in UGPase from different species.

PubMed: 22132858
DOI: 10.1042/BJ20111598

実験手法

X-RAY DIFFRACTION (3.6 Å)