6kqw
Crystal structure of Yijc from B. subtilis
Structural highlights
FunctionNDPGT_BACSU Glycosyltransferase that can glycosylate a wide range of substrates, including various flavonoids, phenyl ketones, curcuminoid, lignins, zingerone, triterpenes, stilbene and anthraquinone, using UDP-glucose or ADP-glucose as sugar donor (PubMed:28315700, PubMed:33152360). It also exhibits O-, N- and S-glycosylation activities towards simple aromatics (PubMed:28315700). In vivo, the broad acceptor tolerance of YjiC might function as a detoxification agent against exogenous xenobiotics to make the strain adaptable to the changeable environment (Probable).[1] [2] [3] Publication Abstract from PubMedGlycosylation catalyzed by uridine diphosphate-dependent glycosyltransferases (UGT) contributes to the chemical and functional diversity of a number of natural products. Bacillus subtilis Bs-YjiC is a robust and versatile UGT that holds potentials in the biosynthesis of unnatural bioactive ginsenosides. To understand the molecular mechanism underlying the substrate promiscuity of Bs-YjiC, we solved crystal structures of Bs-YjiC and its binary complex with uridine diphosphate (UDP) at resolution of 2.18 A and 2.44 A, respectively. Bs-YjiC adopts the classical GT-B fold containing the N-terminal and C-terminal domains that accommodate the sugar acceptor and UDP-glucose, respectively. Molecular docking indicates that the spacious sugar-acceptor binding pocket of Bs-YjiC might be responsible for its broad substrate spectrum and unique glycosylation patterns toward protopanaxadiol-(PPD) and PPD-type ginsenosides. Our study reveals the structural basis for the aglycone promiscuity of Bs-YjiC and will facilitate the protein engineering of Bs-YjiC to synthesize novel bioactive glycosylated compounds. Structural dissection of unnatural ginsenoside-biosynthetic UDP-glycosyltransferase Bs-YjiC from Bacillus subtilis for substrate promiscuity.,Dai L, Qin L, Hu Y, Huang JW, Hu Z, Min J, Sun Y, Guo RT Biochem Biophys Res Commun. 2021 Jan 1;534:73-78. doi:, 10.1016/j.bbrc.2020.11.104. Epub 2020 Dec 10. PMID:33310191[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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