5jvv

Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase

spinqualitylabelsall models 5jvv, resolution 1.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jvv is a 2 chain structure with sequence from Paecilomyces sp. 'thermophila'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.589Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1S4NYE9_9EURO Publication Abstract from PubMed Carbohydrates are complex macromolecules in biological metabolism. Enzymatic synthesis of carbohydrates is recognized as powerful tool to overcome the problems associated with large-scale synthesis of carbohydrates. Novel enzymes with significant transglycosylation ability are still in great demand in glycobiology studies. Here we report a novel glycoside hydrolase (GH) family 16 elongating beta-transglycosylase from Paecilomyces thermophila (PtBgt16A), which efficiently catalyzes the synthesis of higher polymeric oligosaccharides using beta-1,3/1,4 oligosaccharides as donor/acceptor substrates. Further structural information reveals that PtBgt16A own a binding pocket around the -1 subsite. The catalytic mechanism of PtBgt16A is partly similar to an exo- glycoside hydrolase, which cleaves the substrate from the non-reducing end one by one. However, PtBgt16A releases the reducing end product and uses remainder glucosyl as transglycosylation donor. This catalytic mechanism has similarity with the catalytic mode of amylosucrase, which leads the transglycosylation products gradually extend by one glucose unit. PtBgt16A thus has the potential to be a tool enzyme for the enzymatic synthesis of new beta-oligosaccharides and glycoconjugates. Catalytic mechanism of a novel glycoside hydrolase family 16 elongating beta - transglycosylase.,Qin Z, Yang S, Zhao L, You X, Yan Q, Jiang Z J Biol Chem. 2016 Dec 12. pii: jbc.M116.762419. PMID:27956553 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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