2vg8 | pdb_00002vg8

Characterization and engineering of the bifunctional N- and O- glucosyltransferase involved in xenobiotic metabolism in plants

spinqualitylabelsall models 2vg8, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vg8 is a 1 chain structure with sequence from Arath. This structure supersedes the now removed PDB entry 2vcu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, TRS, UDP Related: 2vce, 2vch, 2vcu Activity: Hydroquinone glucosyltransferase, with EC number 2.4.1.218 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [U72B1_ARATH] Bifunctional O-glycosyltransferase and N-glycosyltransferase that can detoxify xenobiotics. Possesses high activity to metabolize the peristent pollutants 2,4,5-trichlorophenol (TCP) and 3,4-dichloroaniline (DCA). Also active on benzoates and benzoate derivatives in vitro. 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 glucosylation of pollutant and pesticide metabolites in plants controls their bioactivity and the formation of subsequent chemical residues. The model plant Arabidopsis thaliana contains >100 glycosyltransferases (GTs) dedicated to small-molecule conjugation and, whereas 44 of these enzymes catalyze the O-glucosylation of chlorinated phenols, only one, UGT72B1, shows appreciable N-glucosylating activity toward chloroanilines. UGT72B1 is a bifunctional O-glucosyltransferase (OGT) and N-glucosyltransferase (NGT). To investigate this unique dual activity, the structure of the protein was solved, at resolutions up to 1.45 A, in various forms including the Michaelis complex with intact donor analog and trichlorophenol acceptor. The catalytic mechanism and basis for O/N specificity was probed by mutagenesis and domain shuffling with an orthologous enzyme from Brassica napus (BnUGT), which possesses only OGT activity. Mutation of BnUGT at just two positions (D312N and F315Y) installed high levels of NGT activity. Molecular modeling revealed the connectivity of these residues to H19 on UGT72B1, with its mutagenesis exclusively defining NGT activity in the Arabidopsis enzyme. These results shed light on the conjugation of nonnatural substrates by plant GTs, highlighting the catalytic plasticity of this enzyme class and the ability to engineer unusual and desirable transfer to nitrogen-based acceptors. Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants.,Brazier-Hicks M, Offen WA, Gershater MC, Revett TJ, Lim EK, Bowles DJ, Davies GJ, Edwards R Proc Natl Acad Sci U S A. 2007 Dec 18;104(51):20238-43. Epub 2007 Dec 12. PMID:18077347 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycosyltransferase 3D structures

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