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Structural modeling of two plant UDP-dependent sugar-sugar glycosyltransferases reveals a conserved glutamic acid residue that is a hallmark for sugar acceptor recognition.
Brandt, Wolfgang; Schulze, Eva; Liberman-Aloni, Raya; Bartelt, Richard; Pienkny, Silke; Carmeli-Weissberg, Mira; Frydman, Ahuva; Eyal, Yoram.
Afiliación
  • Brandt W; Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle (Saale), Germany. Electronic address: drwbra@gmail.com.
  • Schulze E; Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle (Saale), Germany.
  • Liberman-Aloni R; Institute of Plant Sciences, The Volcani Center, ARO, P.O. Box 6, Bet-Dagan, 50250, Israel.
  • Bartelt R; Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle (Saale), Germany.
  • Pienkny S; Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle (Saale), Germany.
  • Carmeli-Weissberg M; Institute of Plant Sciences, The Volcani Center, ARO, P.O. Box 6, Bet-Dagan, 50250, Israel.
  • Frydman A; Institute of Plant Sciences, The Volcani Center, ARO, P.O. Box 6, Bet-Dagan, 50250, Israel.
  • Eyal Y; Institute of Plant Sciences, The Volcani Center, ARO, P.O. Box 6, Bet-Dagan, 50250, Israel. Electronic address: eyalab@volcani.agri.gov.il.
J Struct Biol ; 213(3): 107777, 2021 09.
Article en En | MEDLINE | ID: mdl-34391905
Glycosylation is one of the common modifications of plant metabolites, playing a major role in the chemical/biological diversity of a wide range of compounds. Plant metabolite glycosylation is catalyzed almost exclusively by glycosyltransferases, mainly by Uridine-diphosphate dependent Glycosyltransferases (UGTs). Several X-ray structures have been determined for primary glycosyltransferases, however, little is known regarding structure-function aspects of sugar-sugar/branch-forming O-linked UGTs (SBGTs) that catalyze the transfer of a sugar from the UDP-sugar donor to an acceptor sugar moiety of a previously glycosylated metabolite substrate. In this study we developed novel insights into the structural basis for SBGT catalytic activity by modelling the 3d-structures of two enzymes; a rhamnosyl-transferase Cs1,6RhaT - that catalyzes rhamnosylation of flavonoid-3-glucosides and flavonoid-7-glucosides and a UGT94D1 - that catalyzes glucosylation of (+)-Sesaminol 2-O-ß-d-glucoside at the C6 of the primary sugar moiety. Based on these structural models and docking studies a glutamate (E290 or E268 in Cs1,6RhaT or UGT94D1, respectively) and a tryptophan (W28 or W15 in Cs1,6RhaT or UGT94D1, respectively) appear to interact with the sugar acceptor and are suggested to be important for the recognition of the sugar-moiety of the acceptor-substrate. Functional analysis of substitution mutants for the glutamate and tryptophan residues in Cs1,6RhaT further support their role in determining sugar-sugar/branch-forming GT specificity. Phylogenetic analysis of the UGT family in plants demonstrates that the glutamic-acid residue is a hallmark of SBGTs that is entirely absent from the corresponding position in primary UGTs.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Uridina Difosfato / Glicosiltransferasas Idioma: En Revista: J Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Uridina Difosfato / Glicosiltransferasas Idioma: En Revista: J Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article Pais de publicación: Estados Unidos