Structural Dissection Of Unnatural Ginsenoside-Biosynthetic Udp-Glycosyltransferase Bs-Yjic From Bacillus Subtilis For Substrate Promiscuity
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS(2021)
摘要
Glycosylation 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 angstrom and 2.44 angstrom, 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. (C) 2020 Elsevier Inc. All rights reserved.
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关键词
Glycosyltransferase, Bs-YjiC, Uridine diphosphate-dependent glycosyltransferase, Unnatural ginsenoside biosynthesis, Crystal structure
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