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The Structure of Bacillus subtilis glycosyltransferase,Bs-YjiC
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 possess prominent biological and pharmacological significance in natural product and drug candidate synthesis. The glycosyltransferase YjiC, discovered from Bacillus subtilis (Bs-YjiC), shows potential applications in drug development due to its wide substrate spectrums. In order to elucidate its catalytic mechanism, we solved the crystal structure of Bs-YjiC, demonstrating that Bs-YjiC adopts a typical GT-B fold consisting of a flexible N-domain and a relatively rigid C-domain. Structural analysis coupled with site-directed mutagenesis studies revealed that site Ser277 was critical for Nucleoside Diphosphate (NDP) recognition, while Glu317, Gln318, Ser128 and Ser129 were crucial for glycosyl moiety recognition. Our results illustrate the structural basis for acceptor promiscuity in Bs-YjiC and provide a starting point for further protein engineering of Bs-YjiC in industrial and pharmaceutical applications. Structural and biochemical studies of the glycosyltransferase Bs-YjiC from Bacillus subtilis.,Liu B, Zhao C, Xiang Q, Zhao N, Luo Y, Bao R Int J Biol Macromol. 2021 Jan 1;166:806-817. doi: 10.1016/j.ijbiomac.2020.10.238., Epub 2020 Nov 2. PMID:33152360[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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