Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 27199480Publication DOI: 10.1073/pnas.1603146113Journal NLM ID: 7505876Publisher: National Academy of Sciences
Correspondence: mkimber
uoguelph.ca; cwhitfie
uoguelph.ca
Institutions: Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON, Canada N1G 2W1, Department of Chemistry and Alberta Glycomics Centre, University of Alberta, Edmonton, AB, Canada
Kdo (3-deoxy-d-manno-oct-2-ulosonic acid) is an eight-carbon sugar mostly confined to Gram-negative bacteria. It is often involved in attaching surface polysaccharides to their lipid anchors. α-Kdo provides a bridge between lipid A and the core oligosaccharide in all bacterial LPSs, whereas an oligosaccharide of β-Kdo residues links 'group 2' capsular polysaccharides to (lyso)phosphatidylglycerol. β-Kdo is also found in a small number of other bacterial polysaccharides. The structure and function of the prototypical cytidine monophosphate-Kdo-dependent α-Kdo glycosyltransferase from LPS assembly is well characterized. In contrast, the β-Kdo counterparts were not identified as glycosyltransferase enzymes by bioinformatics tools and were not represented among the 98 currently recognized glycosyltransferase families in the Carbohydrate-Active Enzymes database. We report the crystallographic structure and function of a prototype β-Kdo GT from WbbB, a modular protein participating in LPS O-antigen synthesis in Raoultella terrigena The β-Kdo GT has dual Rossmann-fold motifs typical of GT-B enzymes, but extensive deletions, insertions, and rearrangements result in a unique architecture that makes it a prototype for a new GT family (GT99). The cytidine monophosphate-binding site in the C-terminal alpha/beta domain closely resembles the corresponding site in bacterial sialyltransferases, suggesting an evolutionary connection that is not immediately evident from the overall fold or sequence similarities.
polysaccharide, 3-deoxy-D-manno-oct-2-ulosonic acid, Kdo, glycosyltransferase, Raoultella terrigena, microbial glycobiology
Structure type: polymer chemical repeating unit
Location inside paper: p.E3122, fig.2, E. coli K-14
Trivial name: K-antigen
Compound class: CPS
Contained glycoepitopes: IEDB_130648,IEDB_137473
Methods: 13C NMR, 1H NMR, NMR-2D, PCR, DNA sequencing, SDS-PAGE, TLC, chemical synthesis, genetic methods, crystallography, FPLC, LC-MS, bioinformatic analysis, phylogenetic analysis
Biological activity: the structure and function of a prototype β-Kdo transferase
Biosynthesis and genetic data: genetic data
3D data: 3D data
Related record ID(s): 11309, 11696, 11697, 11698, 11699, 11700, 11701, 11702, 11703, 11704, 11705, 11706, 11707, 11708, 11709, 11710
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure:
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