Evidence map›Paper›PMID 37591902›Full record

ArticleScientific reports2023

Molecular modelling and site-directed mutagenesis provide insight into saccharide pyruvylation by the Paenibacillus alvei CsaB enzyme.

Cordula Stefanović, Fiona F Hager-Mair, Erik Breslmayr, Arturo López-Guzmán, Charlie Lim, Markus Blaukopf, Paul Kosma, Chris Oostenbrink, Roland Ludwig, Christina Schäffer

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 66% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

10 authors at 2 institutions in 1 country.

Cordula Stefanović *NanoGlycobiology Research Group, Department of Chemistry, Institute of Biochemistry, Universität für Bodenkultur Wien, Muthgasse 18, 1190, Vienna, Austria.
Fiona F Hager-Mair *NanoGlycobiology Research Group, Department of Chemistry, Institute of Biochemistry, Universität für Bodenkultur Wien, Muthgasse 18, 1190, Vienna, Austria.
Erik BreslmayrDepartment of Food Science and Technology, Biocatalysis and Biosensing Laboratory, Universität für Bodenkultur Wien, Muthgasse 11, 1190, Vienna, Austria.
Arturo López-GuzmánNanoGlycobiology Research Group, Department of Chemistry, Institute of Biochemistry, Universität für Bodenkultur Wien, Muthgasse 18, 1190, Vienna, Austria.
Charlie LimDepartment of Chemistry, Institute of Organic Chemistry, Universität für Bodenkultur Wien, Muthgasse 18, 1190, Vienna, Austria.
Markus BlaukopfDepartment of Chemistry, Institute of Organic Chemistry, Universität für Bodenkultur Wien, Muthgasse 18, 1190, Vienna, Austria.
Paul KosmaDepartment of Chemistry, Institute of Organic Chemistry, Universität für Bodenkultur Wien, Muthgasse 18, 1190, Vienna, Austria.
Chris OostenbrinkDepartment of Material Sciences and Process Engineering, Institute for Molecular Modelling and Simulation, Universität für Bodenkultur Wien, Muthgasse 18, 1190, Vienna, Austria.
Roland LudwigDepartment of Food Science and Technology, Biocatalysis and Biosensing Laboratory, Universität für Bodenkultur Wien, Muthgasse 11, 1190, Vienna, Austria.
Christina SchäfferNanoGlycobiology Research Group, Department of Chemistry, Institute of Biochemistry, Universität für Bodenkultur Wien, Muthgasse 18, 1190, Vienna, Austria. christina.schaeffer@boku.ac.at.
BOKU University · ATVRVis GmbH (Austria) · AT

Funding

Austrian Science Fund FWF P 32521Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Pyruvylation is a biologically versatile but mechanistically unexplored saccharide modification. 4,6-Ketal pyruvylated N-acetylmannosamine within bacterial secondary cell wall polymers serves as a cell wall anchoring epitope for proteins possessing a terminal S-layer homology domain trimer. The pyruvyltransferase CsaB from Paenibacillus alvei served as a model to investigate the structural basis of the pyruvyltransfer reaction by a combination of molecular modelling and site-directed mutagenesis together with an enzyme assay using phosphoenolpyruvate (PEP; donor) and synthetic β-D-ManNAc-(1 → 4)-α-D-GlcNAc-diphosphoryl-11-phenoxyundecyl (acceptor). CsaB protein structure modelling was done using Phyre2 and I-Tasser based on the partial crystal structure of the Schizosaccharomyces pombe pyruvyltransferase Pvg1p and by AlphaFold. The models informed the construction of twelve CsaB mutants targeted at plausible PEP and acceptor binding sites and K

Indexed as

BacillusPaenibacillusBinding SitesMutagenesis, Site-Directed

Identifiers

PMID37591902
PMCPMC10435577
OpenAlexW4385950787

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.