7SHG

Polysaccharide ribofuranosyl transferase from Thermobacillus composti

Summary for 7SHG

• Entry DOI: 10.2210/pdb7shg/pdb
• Descriptor: Ribofuranosyl transferase, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: glycosyltransferase, phosphatase, ribofuranose, transferase
• Biological source: Thermobacillus composti
• Total number of polymer chains: 2
• Total formula weight: 152961.95

Authors

Kimber, M.S.,Kelly, S.D. (deposition date: 2021-10-08, release date: 2022-03-02, Last modification date: 2024-04-03)

Primary citation

Kelly, S.D.,Williams, D.M.,Nothof, J.T.,Kim, T.,Lowary, T.L.,Kimber, M.S.,Whitfield, C.
The biosynthetic origin of ribofuranose in bacterial polysaccharides.
Nat.Chem.Biol., 18:530-537, 2022

PubMed Abstract: 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-α-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-Å 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.

PubMed: 35393575
DOI: 10.1038/s41589-022-01006-6

Experimental method

X-RAY DIFFRACTION (2.5 Å)