5tme

Crystal structure of Os79 from O. sativa in complex with UDP.

spinqualitylabelsall models 5tme, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tme is a 1 chain structure with sequence from Oryza sativa Japonica Group. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.78Å Ligands: UDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UGT79_ORYSJ Involved in the detoxification of the Fusarium mycotoxin deoxynivalenol by the transfer of glucose from UDP-D-glucose to the hydroxyl group at C-3, forming deoxynivalenol-3-O-beta-D-glucoside. Publication Abstract from PubMed Fusarium head blight is a plant disease with significant agricultural and health impacts which affects cereal crops such as wheat, barley, and maize, and is characterized by reduced grain yield and the accumulation of trichothecene mycotoxins such as deoxynivalenol (DON). Studies have identified trichothecene production as a virulence factor in Fusarium graminearum, and have linked DON resistance to the ability to form DON-3-O-glucoside in wheat. Here, the structures of a deoxynivalenol:UDP-glucosyltransferase (Os79) from Oryza sativa are reported in complex with UDP in an open conformation, in complex with UDP in a closed conformation, and in complex with UDP-2-fluoro-2-deoxy-D-glucose and trichothecene at 1.8, 2.3, and 2.2 A resolution respectively. The active site of Os79 lies in a groove between the N-terminal acceptor and the C-terminal donor-binding domains. Structural alignments reveal that Os79 likely utilizes a catalytic mechanism similar to other plant UGTs, with His 27 activating the trichothecene O3 hydroxyl for nucleophilic attack at C1 of the UDP-glucose donor. Kinetic analysis of mutant Os79 revealed that Thr 291 plays a critical role in catalysis as either a catalytic acid or to position the UDP moiety during the nucleophilic attack. Steady-state kinetic analysis demonstrated that Os79 conjugates multiple trichothecene substrates such as DON, nivalenol, isotrichodermol, and HT-2 toxin, but not T-2 toxin. These data establish a foundation for understanding substrate specificity and activity in this enzyme, and can be used to guide future efforts to increase DON resistance in cereal crops. Crystal structure of Os79 (Os04g0206600) from Oryza sativa: A UDP-glucosyltransferase involved in the detoxification of deoxynivalenol.,Wetterhorn KM, Newmister SA, Caniza RK, Busman M, McCormick SP, Berthiller F, Adam G, Rayment I Biochemistry. 2016 Oct 7. PMID:27715009 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycosyltransferase 3D structures

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