ArticleThe Journal of biological chemistry2014
Structure of a novel O-linked N-acetyl-D-glucosamine (O-GlcNAc) transferase, GtfA, reveals insights into the glycosylation of pneumococcal serine-rich repeat adhesins.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed, 54 citations in OpenAlex.
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- A protein O-GlcNAc glycosyltransferase regulates the antioxidative response in Yersinia pestis.Nature communications · 2024Article
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- The role of O-GlcNAcylation in bone metabolic diseases.Frontiers in physiology · 2024Review
- Pneumococcal Surface Proteins as Virulence Factors, Immunogens, and Conserved Vaccine Targets.Frontiers in cellular and infection microbiology · 2022Review
- Structural basis for SdgB- and SdgA-mediated glycosylation of staphylococcal adhesive proteins.Acta crystallographica. Section D, Structural biology · 2021Article
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- A Glycolipid Glycosyltransferase with Broad Substrate Specificity from the Marine Bacterium "Applied and environmental microbiology · 2021Article
- Glycosyltransferases within theJournal of bacteriology · 2021Article
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- Serine-rich repeat proteins from gut microbes.Gut microbes · 2020Review
- Identification ofFrontiers in endocrinology · 2019Article
- Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles.Glycobiology · 2019Article
- Structural basis for the glycosyltransferase activity of theThe Journal of biological chemistry · 2018Article
- How Sweet Are Our Gut Beneficial Bacteria? A Focus on Protein Glycosylation in Lactobacillus.International journal of molecular sciences · 2018Review
- Lipoteichoic acid deficiency permits normal growth but impairs virulence of Streptococcus pneumoniae.Nature communications · 2017Article
- O-acetylation of the serine-rich repeat glycoprotein GspB is coordinated with accessory Sec transport.PLoS pathogens · 2017Article
- Defining the enzymatic pathway for polymorphicThe Journal of biological chemistry · 2017Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
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Abstract
Protein glycosylation catalyzed by the O-GlcNAc transferase (OGT) plays a critical role in various biological processes. In Streptococcus pneumoniae, the core enzyme GtfA and co-activator GtfB form an OGT complex to glycosylate the serine-rich repeat (SRR) of adhesin PsrP (pneumococcal serine-rich repeat protein), which is involved in the infection and pathogenesis. Here we report the 2.0 Å crystal structure of GtfA, revealing a β-meander add-on domain beyond the catalytic domain. It represents a novel add-on domain, which is distinct from the all-α-tetratricopeptide repeats in the only two structure-known OGTs. Structural analyses combined with binding assays indicate that this add-on domain contributes to forming an active GtfA-GtfB complex and recognizing the acceptor protein. In addition, the in vitro glycosylation system enables us to map the O-linkages to the serine residues within the first SRR of PsrP. These findings suggest that fusion with an add-on domain might be a universal mechanism for diverse OGTs that recognize varying acceptor proteins/peptides.
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