7xr9

Crystal structure of DgpA with glucose

spinqualitylabelsall models 7xr9, resolution 2.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7xr9 is a 6 chain structure with sequence from Human intestinal bacterium PUE. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.42Å Ligands: BGC, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A3Q9WWX8_UNCXX Publication Abstract from PubMed The C-glycosidic bond that connects the sugar moiety with aglycone is difficult to be broken or made due to its inert nature. The knowledge of C-glycoside breakdown and synthesis is very limited. Recently, the enzyme DgpA/B/C cascade from a human intestinal bacterium PUE was identified to specifically cleave the C-glycosidic bond of puerarin (daidzein-8-C-glucoside). Here we investigated how puerarin is recognized and oxidized by DgpA based on crystal structures of DgpA with or without substrate and biochemical characterization. More strikingly, we found that apart from being a C-glycoside cleaving enzyme, DgpA/B/C is capable of efficiently converting O- to C-glycoside showing the activity as a structure isomerase. A possible mechanistic model was proposed dependently of the simulated complex structure of DgpB/C with 3-oxo-daidzin and structure-based mutagenesis. Our findings not only shed light on understanding the enzyme-mediated C-glycosidic bond breakage and formation, but also may help to facilitate stereospecific C-glycoside synthesis in pharmaceutical industry. Structural mechanism of a dual-functional enzyme DgpA/B/C as both a C-glycoside cleaving enzyme and an O- to C-glycoside isomerase.,He P, Wang S, Li S, Liu S, Zhou S, Wang J, Tao J, Wang D, Wang R, Ma W Acta Pharm Sin B. 2023 Jan;13(1):246-255. doi: 10.1016/j.apsb.2022.05.022. Epub , 2022 May 25. PMID:36815035 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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