3hbj

Structure of UGT78G1 complexed with UDP

spinqualitylabelsall models 3hbj, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hbj is a 1 chain structure with sequence from Barrel medic. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: UDP Related: 3hbf Gene: GT83F, UGT78G1 (Barrel medic) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The glycosyltransferase UGT78G1 from Medicago truncatula catalyzes the glycosylation of various (iso)flavonoids such as the flavonols kaempferol and myricetin, the isoflavone formononetin, and the anthocyanidins pelargonidin and cyanidin. It also catalyzes a reverse reaction to remove the sugar moiety from glycosides. The structures of UGT78G1 bound with uridine diphosphate or with both uridine diphosphate and myricetin were determined at 2.1 A resolution, revealing detailed interactions between the enzyme and substrates/products and suggesting a distinct binding mode for the acceptor/product. Comparative structural analysis and mutagenesis identify glutamate 192 as a key amino acid for the reverse reaction. This information provides a basis for enzyme engineering to manipulate substrate specificity and to design effective biocatalysts with glycosylation and/or deglycosylation activity. Crystal structures of glycosyltransferase UGT78G1 reveal the molecular basis for glycosylation and deglycosylation of (iso)flavonoids.,Modolo LV, Li L, Pan H, Blount JW, Dixon RA, Wang X J Mol Biol. 2009 Oct 9;392(5):1292-302. Epub 2009 Aug 13. PMID:19683002 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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