ArticleNature communications2014
The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 77 citations in OpenAlex.
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- Identification and genetic engineering of pneumococcal capsule-like polysaccharides in commensal oral streptococci.Microbiology spectrum · 2024Article
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- Identification of a short, single site matriglycan that maintains neuromuscular function in the mouse.bioRxiv : the preprint server for biology · 2023Article
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- Subfunctionalization of a monolignol to a phytoalexin glucosyltransferase is accompanied by substrate inhibition.Plant communications · 2023Article
- Exopolysaccharide Biosynthesis inInternational journal of molecular sciences · 2023Article
- Unraveling the Diverse Roles of Neglected Genes Containing Domains of Unknown Function (DUFs): Progress and Perspective.International journal of molecular sciences · 2023Review
- Subcellular localization of the enterobacterial common antigen GT-E-like glycosyltransferase, WecG.Molecular microbiology · 2022Article
- Contribution of TagA-Like Glycosyltransferases to the Assembly of the Secondary Cell Wall Polysaccharide in Bacillus anthracis.Journal of bacteriology · 2022Article
- The biosynthetic origin of ribofuranose in bacterial polysaccharides.Nature chemical biology · 2022Article
- Mapping the glycosyltransferase fold landscape using interpretable deep learning.Nature communications · 2021Article
- Article
- A bifunctional O-antigen polymerase structure reveals a new glycosyltransferase family.Nature chemical biology · 2020Article
- Type III Secretion Effectors with Arginine N-Glycosyltransferase Activity.Microorganisms · 2020Review
- Bacteria-Catalyzed Arginine Glycosylation in Pathogens and Host.Frontiers in cellular and infection microbiology · 2020Review
- Serine-rich repeat proteins from gut microbes.Gut microbes · 2020Review
- Streptococcal Serine-Rich Repeat Proteins in Colonization and Disease.Frontiers in microbiology · 2020Review
- Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach.International journal of molecular sciences · 2019Review
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
More than 33,000 glycosyltransferases have been identified. Structural studies, however, have only revealed two distinct glycosyltransferase (GT) folds, GT-A and GT-B. Here we report a 1.34-Å resolution X-ray crystallographic structure of a previously uncharacterized 'domain of unknown function' 1792 (DUF1792) and show that the domain adopts a new fold and is required for glycosylation of a family of serine-rich repeat streptococcal adhesins. Biochemical studies reveal that the domain is a glucosyltransferase, and it catalyses the transfer of glucose to the branch point of the hexasaccharide O-linked to the serine-rich repeat of the bacterial adhesin, Fap1 of Streptococcus parasanguinis. DUF1792 homologues from both Gram-positive and Gram-negative bacteria also exhibit the activity. Thus, DUF1792 represents a new family of glycosyltransferases; therefore, we designate it as a GT-D glycosyltransferase fold. As the domain is highly conserved in bacteria and not found in eukaryotes, it can be explored as a new antibacterial target.
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Registered trials
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