ArticleProceedings of the National Academy of Sciences of the United States of America2016
Bacterial β-Kdo glycosyltransferases represent a new glycosyltransferase family (GT99).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 56 citations in OpenAlex.
- O-antigen polysaccharides inMicrobiology and molecular biology reviews : MMBR · 2025Review
- Integrating Subacute Ruminal Acidosis, Lipopolysaccharide, and Trained Immunity: A Comprehensive Review.International journal of biological sciences · 2025Review
- Putative rhamnogalacturonan-II glycosyltransferase identified through callus gene editing which bypasses embryo lethality.Plant physiology · 2024Article
- Klebsiella pneumoniae O-polysaccharide biosynthesis highlights the diverse organization of catalytic modules in ABC transporter-dependent glycan assembly.The Journal of biological chemistry · 2024Article
- The biosynthetic origin of ribofuranose in bacterial polysaccharides.Nature chemical biology · 2022Article
- Bacterial polysaccharides-A big source for prebiotics and therapeutics.Frontiers in nutrition · 2022Review
- Mapping the glycosyltransferase fold landscape using interpretable deep learning.Nature communications · 2021Article
- Side Chain Conformation Restriction in the Catalysis of Glycosidic Bond Formation by Leloir Glycosyltransferases, Glycoside Phosphorylases, and Transglycosidases.ACS catalysis · 2021Article
- Oral and Gut Microbial Carbohydrate-Active Enzymes Landscape in Health and Disease.Frontiers in microbiology · 2021Article
- Nucleotide Sugars in Chemistry and Biology.Molecules (Basel, Switzerland) · 2020Review
- Identification of the Pseudomonas aeruginosa O17 and O15 O-Specific Antigen Biosynthesis Loci Reveals an ABC Transporter-Dependent Synthesis Pathway and Mechanisms of Genetic Diversity.Journal of bacteriology · 2020Article
- Lipopolysaccharide O-antigens-bacterial glycans made to measure.The Journal of biological chemistry · 2020Review
- Chemical structure and genetic organization of the E. coli O6:K15 capsular polysaccharide.Scientific reports · 2020Article
- A bifunctional O-antigen polymerase structure reveals a new glycosyltransferase family.Nature chemical biology · 2020Article
- Structural and mechanistic themes in glycoconjugate biosynthesis at membrane interfaces.Current opinion in structural biology · 2019Review
- Substrate recognition by a carbohydrate-binding module in the prototypical ABC transporter for lipopolysaccharide O-antigen fromThe Journal of biological chemistry · 2019Article
- Biosynthesis of a conserved glycolipid anchor for Gram-negative bacterial capsules.Nature chemical biology · 2019Article
- Reconstruction of the sialylation pathway in the ancestor of eukaryotes.Scientific reports · 2018Article
- X-ray crystallographic structure of a bacterial polysialyltransferase provides insight into the biosynthesis of capsular polysialic acid.Scientific reports · 2017Article
- Single polysaccharide assembly protein that integrates polymerization, termination, and chain-length quality control.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 α/β 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.
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