Evidence map›Paper›PMID 27637560›Full record

ArticleThe Plant cell2016

Structure of Arabidopsis thaliana FUT1 Reveals a Variant of the GT-B Class Fold and Provides Insight into Xyloglucan Fucosylation.

Joana Rocha, Félix Cicéron, Daniele de Sanctis, Mickael Lelimousin, Valérie Chazalet, Olivier Lerouxel, Christelle Breton

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
8.2field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 44 citations in OpenAlex.

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  13. Frontiers in plant science · 2021
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  16. 3D Structure and Function of Glycosyltransferases Involved inInternational journal of molecular sciences · 2020
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Joana RochaUniversité Grenoble Alpes, 38400 Grenoble, France.ORCID 0000-0003-2272-239X
Félix CicéronUniversité Grenoble Alpes, 38400 Grenoble, France.ORCID 0000-0001-7863-4327
Daniele de SanctisESRF-The European Synchrotron, 38000 Grenoble, France.ORCID 0000-0003-0391-8290
Mickael LelimousinUniversité Grenoble Alpes, 38400 Grenoble, France.ORCID 0000-0002-4547-0132
Valérie ChazaletUniversité Grenoble Alpes, 38400 Grenoble, France.
Olivier LerouxelUniversité Grenoble Alpes, 38400 Grenoble, France.ORCID 0000-0002-7633-1792
Christelle BretonUniversité Grenoble Alpes, 38400 Grenoble, France breton@cermav.cnrs.fr.ORCID 0000-0003-3697-0677
Centre National de la Recherche Scientifique · FREuropean Synchrotron Radiation Facility · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The plant cell wall is a complex and dynamic network made mostly of cellulose, hemicelluloses, and pectins. Xyloglucan, the major hemicellulosic component in Arabidopsis thaliana, is biosynthesized in the Golgi apparatus by a series of glycan synthases and glycosyltransferases before export to the wall. A better understanding of the xyloglucan biosynthetic machinery will give clues toward engineering plants with improved wall properties or designing novel xyloglucan-based biomaterials. The xyloglucan-specific α2-fucosyltransferase FUT1 catalyzes the transfer of fucose from GDP-fucose to terminal galactosyl residues on xyloglucan side chains. Here, we present crystal structures of Arabidopsis FUT1 in its apoform and in a ternary complex with GDP and a xylo-oligosaccharide acceptor (named XLLG). Although FUT1 is clearly a member of the large GT-B fold family, like other fucosyltransferases of known structures, it contains a variant of the GT-B fold. In particular, it includes an extra C-terminal region that is part of the acceptor binding site. Our crystal structures support previous findings that FUT1 behaves as a functional dimer. Mutational studies and structure comparison with other fucosyltransferases suggest that FUT1 uses a S

Indexed as

ArabidopsisArabidopsis ProteinsFucosyltransferasesGlucansGolgi ApparatusGuanosine Diphosphate FucoseXylansArabidopsis ProteinsFucosyltransferasesGlucansGuanosine Diphosphate FucoseXylansxyloglucanxyloglucan 2-fucosyltransferase

Identifiers

PMID27637560
PMCPMC5134985
OpenAlexW2519406634

What OpenQuestion holds

Textmetadata
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.