7ery | pdb_00007ery

apo form of the glycosyltransferase

spinqualitylabelsall models 7ery, resolution 1.77Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ery is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 7erx Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Steviol glycosides are the intensely sweet components of extracts from Stevia rebaudiana. These molecules comprise an invariant steviol aglycone decorated with variable glycans and could widely serve as a low-calorie sweetener. However, the most desirable steviol glycosides Reb D and Reb M, devoid of unpleasant aftertaste, are naturally produced only in trace amounts due to low levels of specific beta (1-2) glucosylation in Stevia. Here, we report the biochemical and structural characterization of OsUGT91C1, a glycosyltransferase from Oryza sativa, which is efficient at catalyzing beta (1-2) glucosylation. The enzyme's ability to bind steviol glycoside substrate in three modes underlies its flexibility to catalyze beta (1-2) glucosylation in two distinct orientations as well as beta (1-6) glucosylation. Guided by the structural insights, we engineer this enzyme to enhance the desirable beta (1-2) glucosylation, eliminate beta (1-6) glucosylation, and obtain a promising catalyst for the industrial production of naturally rare but palatable steviol glycosides. Catalytic flexibility of rice glycosyltransferase OsUGT91C1 for the production of palatable steviol glycosides.,Zhang J, Tang M, Chen Y, Ke D, Zhou J, Xu X, Yang W, He J, Dong H, Wei Y, Naismith JH, Lin Y, Zhu X, Cheng W Nat Commun. 2021 Dec 2;12(1):7030. doi: 10.1038/s41467-021-27144-4. PMID:34857750 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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