ArticleProceedings of the National Academy of Sciences of the United States of America2016
Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein.
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 26 papers.
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Who cites it
26 citing papers in PubMed, 36 citations in OpenAlex.
- Comparative study of two xanthan gum glycosyltransferases combining AI structure predictions and molecular modeling.bioRxiv : the preprint server for biology · 2026Article
- Identification of interbacterial adhesion between oral Schaalia species and streptococcal serine-rich repeat glycoproteins.FEMS microbiology letters · 2026Article
- A structural basis for the strain-dependent UDP-sugar specificity of glycosyltransferase C from the Limosilactobacillus reuteri accessory secretion system.Acta crystallographica. Section D, Structural biology · 2025Article
- Multi-omics analysis identified the GmUGT88A1 gene, which coordinately regulates soybean resistance to cyst nematode and isoflavone content.Plant biotechnology journal · 2025Article
- Ultrastructural and glycoproteomic characterization of Prevotella intermedia: Insights into O-glycosylation and outer membrane vesicles.MicrobiologyOpen · 2024Article
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- Structural basis for SdgB- and SdgA-mediated glycosylation of staphylococcal adhesive proteins.Acta crystallographica. Section D, Structural biology · 2021Article
- Optimized Genetic Tools Allow the Biosynthesis of Glycocin F and Analogues Designed To Test the Roles ofJournal of bacteriology · 2021Article
- Semiprocessive Hyperglycosylation of Adhesin by Bacterial ProteinACS chemical biology · 2021Article
- Opportunities and Challenges of Bacterial Glycosylation for the Development of Novel Antibacterial Strategies.Frontiers in microbiology · 2021Review
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- Processivity in Bacterial Glycosyltransferases.ACS chemical biology · 2020Review
- Serine-rich repeat proteins from gut microbes.Gut microbes · 2020Review
- Streptococcal Serine-Rich Repeat Proteins in Colonization and Disease.Frontiers in microbiology · 2020Review
- Membrane trafficking of the bacterial adhesin GspB and the accessory Sec transport machinery.The Journal of biological chemistry · 2019Article
- Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles.Glycobiology · 2019Article
- Critical Review of Plant Cell Wall Matrix Polysaccharide Glycosyltransferase Activities Verified by Heterologous Protein Expression.Frontiers in plant science · 2019Review
- Unraveling the sequence of cytosolic reactions in the export of GspB adhesin fromThe Journal of biological chemistry · 2018Article
- Carb loading takes proteins on a ride.The Journal of biological chemistry · 2018Article
- Characterization of the pgf operon involved in the posttranslational modification of Streptococcus mutans surface proteins.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
O-glycosylation of Ser and Thr residues is an important process in all organisms, which is only poorly understood. Such modification is required for the export and function of adhesin proteins that mediate the attachment of pathogenic Gram-positive bacteria to host cells. Here, we have analyzed the mechanism by which the cytosolic O-glycosyltransferase GtfA/B of Streptococcus gordonii modifies the Ser/Thr-rich repeats of adhesin. The enzyme is a tetramer containing two molecules each of GtfA and GtfB. The two subunits have the same fold, but only GtfA contains an active site, whereas GtfB provides the primary binding site for adhesin. During a first phase of glycosylation, the conformation of GtfB is restrained by GtfA to bind substrate with unmodified Ser/Thr residues. In a slow second phase, GtfB recognizes residues that are already modified with N-acetylglucosamine, likely by converting into a relaxed conformation in which one interface with GtfA is broken. These results explain how the glycosyltransferase modifies a progressively changing substrate molecule.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.