Evidence map›Paper›PMID 24026536›Full record

ArticleOpen biology2013

Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis.

Alexander Striebeck, David A Robinson, Alexander W Schüttelkopf, Daan M F van Aalten

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Fungal-Metal Interactions: A Review of Toxicity and Homeostasis.Journal of fungi (Basel, Switzerland) · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. The yeast protein Gdt1p transports MnThe Journal of biological chemistry · 2018
    Article
  13. HumanProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
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

4 authors at 2 institutions in 1 country.

Alexander StriebeckDivision of Molecular Microbiology, University of Dundee, Dundee DD1 5EH, UK.
David A Robinson
Alexander W Schüttelkopf
Daan M F van Aalten
University of Dundee · GBMRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0900138Wellcome Trust 087590Wellcome Trust WT087590MA
6 · The paper itself

Abstract

The fungal cell possesses an essential carbohydrate cell wall. The outer layer, mannan, is formed by mannoproteins carrying highly mannosylated O- and N-linked glycans. Yeast mannan biosynthesis is initiated by a Golgi-located complex (M-Pol I) of two GT-62 mannosyltransferases, Mnn9p and Van1p, that are conserved in fungal pathogens. Saccharomyces cerevisiae and Candida albicans mnn9 knockouts show an aberrant cell wall and increased antibiotic sensitivity, suggesting the enzyme is a potential drug target. Here, we present the structure of ScMnn9 in complex with GDP and Mn(2+), defining the fold and catalytic machinery of the GT-62 family. Compared with distantly related GT-78/GT-15 enzymes, ScMnn9 carries an unusual extension. Using a novel enzyme assay and site-directed mutagenesis, we identify conserved amino acids essential for ScMnn9 'priming' α-1,6-mannosyltransferase activity. Strikingly, both the presence of the ScMnn9 protein and its product, but not ScMnn9 catalytic activity, are required to activate subsequent ScVan1 processive α-1,6-mannosyltransferase activity in the M-Pol I complex. These results reveal the molecular basis of mannan synthesis and will aid development of inhibitors targeting this process.

Indexed as

Allosteric RegulationAmino Acid SequenceCandida albicansCrystallography, X-RayGuanosine DiphosphateMannansMannosyltransferasesMembrane GlycoproteinsMembrane ProteinsModels, MolecularMolecular Sequence DataProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGuanosine DiphosphateMannansMannosyltransferasesMembrane GlycoproteinsMembrane ProteinsMNN9 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsVAN1 protein, S cerevisiaecell wallglycobiologyglycosyltransferasemannanM-Pol Iprotein crystallography

Identifiers

PMID24026536
PMCPMC3787745
OpenAlexW2095638950

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.