Evidence map›Paper›PMID 29386647›Full record

ArticleNature communications2018

Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase.

Ana S Ramírez, Jérémy Boilevin, Ahmad Reza Mehdipour, Gerhard Hummer, Tamis Darbre, Jean-Louis Reymond, Kaspar P Locher

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. O-antigen polysaccharides inMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  6. Review
  7. FlaG competes with FliS-flagellin complexes for access to FlhA in the flagellar T3SS to controlProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Cryo-EM analysis ofScience advances · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Lipoteichoic acid polymer length is determined by competition between free starter units.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Review
  20. Influence of Protein Glycosylation onFrontiers in microbiology · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Ana S RamírezInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH), CH-8093, Zürich, Switzerland.ORCID http://orcid.org/0000-0002-1619-0721
Jérémy BoilevinDepartment of Chemistry and Biochemistry, University of Berne, CH-3012, Berne, Switzerland.
Ahmad Reza MehdipourDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, DE-60438, Frankfurt, Germany.
Gerhard HummerDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, DE-60438, Frankfurt, Germany.
Tamis DarbreDepartment of Chemistry and Biochemistry, University of Berne, CH-3012, Berne, Switzerland.
Jean-Louis ReymondDepartment of Chemistry and Biochemistry, University of Berne, CH-3012, Berne, Switzerland.ORCID http://orcid.org/0000-0003-2724-2942
Kaspar P LocherInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH), CH-8093, Zürich, Switzerland. locher@mol.biol.ethz.ch.ORCID http://orcid.org/0000-0002-8207-2889

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The membrane-associated, processive and retaining glycosyltransferase PglH from Campylobacter jejuni is part of the biosynthetic pathway of the lipid-linked oligosaccharide (LLO) that serves as the glycan donor in bacterial protein N-glycosylation. Using an unknown counting mechanism, PglH catalyzes the transfer of exactly three α1,4 N-acetylgalactosamine (GalNAc) units to the growing LLO precursor, GalNAc-α1,4-GalNAc-α1,3-Bac-α1-PP-undecaprenyl. Here, we present crystal structures of PglH in three distinct states, including a binary complex with UDP-GalNAc and two ternary complexes containing a chemo-enzymatically generated LLO analog and either UDP or synthetic, nonhydrolyzable UDP-CH

Indexed as

Bacterial ProteinsBinding SitesCampylobacter jejuniGlycosyltransferasesLipopolysaccharidesMolecular Dynamics SimulationProtein ConformationBacterial ProteinsGlycosyltransferaseslipid-linked oligosaccharidesLipopolysaccharides

Identifiers

PMID29386647
PMCPMC5792488

What OpenQuestion holds

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Registered trials

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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.