6ij7 | pdb_00006ij7

Crystal Structure of Arabidopsis thaliana UGT89C1

spinqualitylabelsall models 6ij7, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ij7 is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.701Å Ligands: EDO, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function U89C1_ARATH Flavonol 7-O-rhamnosyltransferase that acts on kaempferol 3-O-glucoside and other 3-O-glycosylated flavonols like quercetin 3-O-glucoside, quercetin 3-O-galactoside and isorhamnetin 3-O-glucoside. Shows a strict specificity for UDP-rhamnose as donor and does not act on flavonol aglycones or 3-O-glycosylated anthocyanins. Publication Abstract from PubMed Glycosylation is a key modification for most molecules including plant natural products, for example, flavonoids and isoflavonoids, and can enhance the bioactivity and bioavailability of the natural products. The crystal structure of plant rhamnosyltransferase UGT89C1 from Arabidopsis thaliana was determined, and the structures of UGT89C1 in complexes with UDP-beta-l-rhamnose and acceptor quercetin revealed the detailed interactions between the enzyme and its substrates. Structural and mutational analysis indicated that Asp356, His357, Pro147 and Ile148 are key residues for sugar donor recognition and specificity for UDP-beta-l-rhamnose. The mutant H357Q exhibited activity with both UDP-beta-l-rhamnose and UDP-glucose. Structural comparison and mutagenesis confirmed that His21 is a key residue as the catalytic base and the only catalytic residue involved in catalysis independently as UGT89C1 lacks the other catalytic Asp that is highly conserved in other reported UGTs and forms a hydrogen bond with the catalytic base His. Ser124 is located in the corresponding position of the catalytic Asp in other UGTs and is not able to form a hydrogen bond with His21. Mutagenesis further showed that Ser124 may not be important in its catalysis, suggesting that His21 and acceptor may form an acceptor-His dyad and UGT89C1 utilizes a catalytic dyad in catalysis instead of catalytic triad. The information of structure and mutagenesis provides structural insights into rhamnosyltransferase substrate specificity and rhamnosylation mechanism. Crystal structures of rhamnosyltransferase UGT89C1 from Arabidopsis thaliana reveal the molecular basis of sugar donor specificity for UDP-beta-l-rhamnose and rhamnosylation mechanism.,Zong G, Fei S, Liu X, Li J, Gao Y, Yang X, Wang X, Shen Y Plant J. 2019 Jul;99(2):257-269. doi: 10.1111/tpj.14321. Epub 2019 Apr 22. PMID:30893500 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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