3R2W

Crystal Structure of UDP-glucose Pyrophosphorylase of Homo Sapiens

Summary for 3R2W

• Entry DOI: 10.2210/pdb3r2w/pdb
• Descriptor: UTP--glucose-1-phosphate uridylyltransferase (1 entity in total)
• Functional Keywords: homo sapiens, rossmann fold beta barrel, nucleotidyltransferase, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 236737.61

Authors

Zheng, X.,Yu, Q. (deposition date: 2011-03-14, release date: 2012-02-08, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.6 Å)