Evidence map›Paper›PMID 21515584›Full record

ArticleGlycobiology2011

Distantly related plant and nematode core α1,3-fucosyltransferases display similar trends in structure-function relationships.

Peter Both, Lukas Sobczak, Christelle Breton, Stephan Hann, Katharina Nöbauer, Katharina Paschinger, Stanislav Kozmon, Ján Mucha, Iain B H Wilson

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 34 citations in OpenAlex.

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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

9 authors at 4 institutions in 3 countries.

Peter BothDepartment of Glycobiology, Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská Cesta 9, Bratislava, Slovakia.
Lukas Sobczak
Christelle Breton
Stephan Hann
Katharina Nöbauer
Katharina Paschinger
Stanislav Kozmon
Ján Mucha
Iain B H Wilson
BOKU University · ATInstitute of Chemistry of the Slovak Academy of Sciences · SKCentre National de la Recherche Scientifique · FRUniversity of Veterinary Medicine Vienna · AT

Funding

Austrian Science Fund FWF P 18447
6 · The paper itself

Abstract

Here, we present a comparative structure-function study of a nematode and a plant core α1,3-fucosyltransferase based on deletion and point mutations of the coding regions of Caenorhabditis elegans FUT-1 and Arabidopsis thaliana FucTA (FUT11). In particular, our results reveal a novel "first cluster motif" shared by both core and Lewis-type α1,3-fucosyltransferases of the GT10 family. To evaluate the role of the conserved serine within this motif, this residue was replaced with alanine in FucTA (S218) and FUT-1 (S243). The S218A replacement completely abolished the enzyme activity of FucTA, while the S243A mutant of FUT-1 retained 20% of the "wild-type" activity. Based on the results of homology modeling of FucTA, other residues potentially involved in the donor substrate binding were examined, and mutations of N219 and R226 dramatically affected enzymatic activity. Finally, as both FucTA and FUT-1 were shown to be N-glycosylated, we examined the putative N-glycosylation sites. While alanine replacements at single potential N-glycosylation sites of FucTA resulted in a loss of up to 80% of the activity, a triple glycosylation site mutant still retained 5%, as compared to the control. In summary, our data indicate similar trends in structure-function relationships of distantly related enzymes which perform similar biochemical reactions and form the basis for future work aimed at understanding the structure of α1,3-fucosyltransferases in general.

Indexed as

Amino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionAnimalsArabidopsisBinding SitesCaenorhabditis elegansCations, DivalentConserved SequenceEnzyme AssaysFucosyltransferasesGlycosylationMagnesiumModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedCations, DivalentFucosyltransferasesgalactoside 3-fucosyltransferaseMagnesiumPeptide FragmentsRecombinant Proteins

Identifiers

PMID21515584
PMCPMC3272405
OpenAlexW2131101991

What OpenQuestion holds

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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.