4.8 Article

The biosynthetic origin of ribofuranose in bacterial polysaccharides

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NATURE CHEMICAL BIOLOGY
卷 18, 期 5, 页码 530-+

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NATURE PORTFOLIO
DOI: 10.1038/s41589-022-01006-6

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资金

  1. Natural Sciences and Engineering Research Council [RGPIN-2020-07113, RGPIN-2018-04365, RGPIN-2020-03886]
  2. Natural Sciences and Engineering Research Council Postgraduate Scholarship
  3. Ontario Graduate Scholarship

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Bacterial surface polysaccharides are synthesized by glycosyltransferases using sugar nucleotide or activated donors. This study identified dual-domain ribofuranosyltransferase proteins that catalyze a two-step reaction sequence for ribofuranose residues found in some polysaccharides. The discovery of these proteins provides insights into the synthesis and function of bacterial polysaccharides.
Bacterial surface polysaccharides are assembled by glycosyltransferase enzymes that typically use sugar nucleotide or polyprenyl-monophosphosugar activated donors. Characterized representatives exist for many monosaccharides but neither the donor nor the corresponding glycosyltransferases have been definitively identified for ribofuranose residues found in some polysaccharides. Klebsiella pneumoniae O-antigen polysaccharides provided prototypes to identify dual-domain ribofuranosyltransferase proteins catalyzing a two-step reaction sequence. Phosphoribosyl-5-phospho-D-ribosyl-alpha-1-diphosphate serves as the donor for a glycan acceptor-specific phosphoribosyl transferase (gPRT), and a more promiscuous phosphoribosyl-phosphatase (PRP) then removes the residual 5'-phosphate. The 2.5-angstrom resolution crystal structure of a dual-domain ribofuranosyltransferase ortholog from Thermobacillus composti revealed a PRP domain that conserves many features of the phosphatase members of the haloacid dehalogenase family, and a gPRT domain that diverges substantially from all previously characterized phosphoribosyl transferases. The gPRT represents a new glycosyltransferase fold conserved in the most abundant ribofuranosyltransferase family.

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