2vce
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The glucosylation of pollutant and pesticide metabolites in plants | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Hydroquinone glucosyltransferase]] | [[Category: Hydroquinone glucosyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bowles, D | + | [[Category: Bowles, D J.]] |
[[Category: Brazier-Hicks, M.]] | [[Category: Brazier-Hicks, M.]] | ||
| - | [[Category: Davies, G | + | [[Category: Davies, G J.]] |
[[Category: Edwards, R.]] | [[Category: Edwards, R.]] | ||
| - | [[Category: Gershater, M | + | [[Category: Gershater, M C.]] |
| - | [[Category: Lim, E | + | [[Category: Lim, E K.]] |
| - | [[Category: Offen, W | + | [[Category: Offen, W A.]] |
| - | [[Category: Revett, T | + | [[Category: Revett, T J.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: TC7]] | [[Category: TC7]] | ||
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[[Category: udp-glucose- dependent]] | [[Category: udp-glucose- dependent]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:55:01 2008'' |
Revision as of 16:55, 21 February 2008
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CHARACTERIZATION AND ENGINEERING OF THE BIFUNCTIONAL N- AND O-GLUCOSYLTRANSFERASE INVOLVED IN XENOBIOTIC METABOLISM IN PLANTS
Overview
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.
About this Structure
2VCE is a Single protein structure of sequence from Arabidopsis thaliana with , and as ligands. Active as Hydroquinone glucosyltransferase, with EC number 2.4.1.218 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 18:55:01 2008
Categories: Arabidopsis thaliana | Hydroquinone glucosyltransferase | Single protein | Bowles, D J. | Brazier-Hicks, M. | Davies, G J. | Edwards, R. | Gershater, M C. | Lim, E K. | Offen, W A. | Revett, T J. | EDO | TC7 | U2F | Glycosyltransferase | N-glucosyltransferase | N-glycosylation | O- glucosyltransferase | O-glycosylation | Plant glycosylation | S-glucosyltransferase | Transferase | Udp-glucose- dependent
