3r2w | pdb_00003r2w

Crystal Strucutre of UDP-glucose Pyrophosphorylase of Homo Sapiens

spinqualitylabelsall models 3r2w, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3r2w is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: UGP2, UGP1 (Homo sapiens) Activity: UTP--glucose-1-phosphate uridylyltransferase, with EC number 2.7.7.9 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed UDP-glucose pyrophosphorylase (UGPase) is highly conserved among eukaryotes. UGPase reversely catalyzes 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. Here the crystal structure of human UGPase (hUGPase) was determined and shown to form octamers through end-to-end and side-by-side interactions. The observed latch loop in hUGPase distinctly differs from yeast UGPase (yUGPase), 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. The crystal structure of human UDP-glucose pyrophosphorylase reveals a latch effect that influence enzymatic activity.,Yu Q, Zheng X Biochem J. 2011 Dec 1. PMID:22132858 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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