3HBF

Structure of UGT78G1 complexed with myricetin and UDP

Summary for 3HBF

• Entry DOI: 10.2210/pdb3hbf/pdb
• Related: 3HBJ
• Descriptor: Flavonoid 3-O-glucosyltransferase, URIDINE-5'-DIPHOSPHATE, 3,5,7-TRIHYDROXY-2-(3,4,5-TRIHYDROXYPHENYL)-4H-CHROMEN-4-ONE, ... (4 entities in total)
• Functional Keywords: glycosyltransferase, gt-b fold, gt1, phenylpropanoid metabolism, transferase
• Biological source: Medicago truncatula (Barrel medic)
• Total number of polymer chains: 1
• Total formula weight: 50938.00

Authors

Wang, X.,Modolo, L.,Li, L.,Dixon, R. (deposition date: 2009-05-04, release date: 2009-09-01, Last modification date: 2024-02-21)

Primary citation

Modolo, L.V.,Li, L.,Pan, H.,Blount, J.W.,Dixon, R.A.,Wang, X.
Crystal structures of glycosyltransferase UGT78G1 reveal the molecular basis for glycosylation and deglycosylation of (iso)flavonoids.
J.Mol.Biol., 392:1292-1302, 2009

PubMed Abstract: 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.

PubMed: 19683002
DOI: 10.1016/j.jmb.2009.08.017

Experimental method

X-RAY DIFFRACTION (2.1 Å)