ArticleScientific reports2018
Structure of bacterial oligosaccharyltransferase PglB bound to a reactive LLO and an inhibitory peptide.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Structural characterisation of the fungal Pmt4 homodimer.Nature communications · 2025Article
- Targeting DDOST improves the efficacy of lenvatinib and immunotherapy in hepatocellular carcinoma.Experimental & molecular medicine · 2025Article
- Atomistic modeling of lysophospholipids from the Campylobacter jejuni lipidome.Biophysical journal · 2025Article
- Characterizing and engineering post-translational modifications with high-throughput cell-free expression.Nature communications · 2025Article
- Structural insights into terminal arabinosylation of mycobacterial cell wall arabinan.Nature communications · 2025Article
- Mechanistic studies of mycobacterial glycolipid biosynthesis by the mannosyltransferase PimE.Nature communications · 2025Article
- Structural insights into polyisoprenyl-binding glycosyltransferases.Structure (London, England : 1993) · 2025Review
- CHARMM-GUI QM/MM Interfacer for a Quantum Mechanical and Molecular Mechanical (QM/MM) Simulation Setup: 1. Semiempirical Methods.Journal of chemical theory and computation · 2024Article
- Recent advances in the biosynthesis of polysaccharide-based antimicrobial glycoconjugate vaccines.Frontiers in microbiology · 2024Review
- Structural and mechanistic studies of the N-glycosylation machinery: from lipid-linked oligosaccharide biosynthesis to glycan transfer.Glycobiology · 2023Review
- Cell-freeFrontiers in molecular biosciences · 2023Article
- Molecular basis for glycan recognition and reaction priming of eukaryotic oligosaccharyltransferase.Nature communications · 2022Article
- Site-to-site cross-talk in OST-B glycosylation of hCEACAM1-IgV.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Carbohydrate-active enzymes (CAZymes) in the gut microbiome.Nature reviews. Microbiology · 2022Review
- Production of Vaccines Using Biological Conjugation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Semiprocessive Hyperglycosylation of Adhesin by Bacterial ProteinACS chemical biology · 2021Article
- Recent Progress in Structural Studies on the GT-C Superfamily of Protein Glycosyltransferases.Sub-cellular biochemistry · 2021Review
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria.Molecular cell · 2020Article
- Structural Insight into the Mechanism ofBiomolecules · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oligosaccharyltransferase (OST) is a key enzyme of the N-glycosylation pathway, where it catalyzes the transfer of a glycan from a lipid-linked oligosaccharide (LLO) to an acceptor asparagine within the conserved sequon N-X-T/S. A previous structure of a ternary complex of bacterial single subunit OST, PglB, bound to a non-hydrolyzable LLO analog and a wild type acceptor peptide showed how both substrates bind and how an external loop (EL5) of the enzyme provided specific substrate-binding contacts. However, there was a relatively large separation of the substrates at the active site. Here we present the X-ray structure of PglB bound to a reactive LLO analog and an inhibitory peptide, revealing previously unobserved interactions in the active site. We found that the atoms forming the N-glycosidic bond (C-1 of the GlcNAc moiety of LLO and the -NH
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.