Evidence map›Paper›PMID 31932718›Full record

ArticleNature chemical biology2020

A fungal family of lytic polysaccharide monooxygenase-like copper proteins.

Aurore Labourel, Kristian E H Frandsen, Feng Zhang, Nicolas Brouilly, Sacha Grisel, Mireille Haon, Luisa Ciano, David Ropartz, Mathieu Fanuel, Francis Martin and 10 more

Open access · greenAbstract read
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In one paragraph

Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
14.8field-weighted citation impact, top 1% 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

37 citing papers in PubMed, 75 citations in OpenAlex.

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  18. GPI-Anchored Protein HomologJournal of fungi (Basel, Switzerland) · 2022
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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

20 authors at 7 institutions in 5 countries.

Aurore LabourelINRA, Biodiversité et Biotechnologie Fongiques (BBF), UMR1163, Aix Marseille Université, Marseille, France.ORCID http://orcid.org/0000-0002-4762-5804
Kristian E H FrandsenINRA, Biodiversité et Biotechnologie Fongiques (BBF), UMR1163, Aix Marseille Université, Marseille, France.
Feng ZhangINRA, UMR1136, Interactions Arbres/Microorganismes, Laboratoire d'Excellence ARBRE, Centre INRA-Lorraine, Université de Lorraine, Champenoux, France.
Nicolas BrouillyCNRS, IBDM, Aix Marseille Université, Marseille, France.
Sacha GriselINRA, Biodiversité et Biotechnologie Fongiques (BBF), UMR1163, Aix Marseille Université, Marseille, France.
Mireille HaonINRA, Biodiversité et Biotechnologie Fongiques (BBF), UMR1163, Aix Marseille Université, Marseille, France.
Luisa CianoDepartment of Chemistry, University of York, York, UK.ORCID http://orcid.org/0000-0002-1667-0856
David RopartzINRA, Unité de Recherche Biopolymères Interactions Assemblages (BIA), Nantes, France.ORCID http://orcid.org/0000-0003-4767-6940
Mathieu FanuelINRA, Unité de Recherche Biopolymères Interactions Assemblages (BIA), Nantes, France.
Francis MartinINRA, UMR1136, Interactions Arbres/Microorganismes, Laboratoire d'Excellence ARBRE, Centre INRA-Lorraine, Université de Lorraine, Champenoux, France.
David NavarroINRA, Biodiversité et Biotechnologie Fongiques (BBF), UMR1163, Aix Marseille Université, Marseille, France.
Marie-Noëlle RossoINRA, Biodiversité et Biotechnologie Fongiques (BBF), UMR1163, Aix Marseille Université, Marseille, France.ORCID http://orcid.org/0000-0001-8317-7220
Tobias TandrupBiological Chemistry Section, Department of Chemistry, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0002-3448-7019
Bastien BissaroINRA, Biodiversité et Biotechnologie Fongiques (BBF), UMR1163, Aix Marseille Université, Marseille, France.
Katja S JohansenDepartment of Geosciences and Natural Resource Management, University of Copenhagen, Copenhagen, Denmark.
Anastasia ZervaINRA, Biodiversité et Biotechnologie Fongiques (BBF), UMR1163, Aix Marseille Université, Marseille, France.ORCID http://orcid.org/0000-0003-0361-7690
Paul H WaltonDepartment of Chemistry, University of York, York, UK.ORCID http://orcid.org/0000-0002-1152-1480
Bernard HenrissatINRA, USC1408 Architecture et Fonction des Macromolécules Biologiques (AFMB), Marseille, France.
Leila Lo LeggioBiological Chemistry Section, Department of Chemistry, University of Copenhagen, Copenhagen, Denmark.ORCID http://orcid.org/0000-0002-5135-0882
Jean-Guy BerrinINRA, Biodiversité et Biotechnologie Fongiques (BBF), UMR1163, Aix Marseille Université, Marseille, France. jean-guy.berrin@inra.fr.ORCID http://orcid.org/0000-0001-7570-3745
Aix-Marseille Université · FRInstitut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement · FRUniversity of Copenhagen · DKCentre National de la Recherche Scientifique · FRUniversity of York · GBBiodiversité et Biotechnologie Fongiques · FRNational Technical University of Athens · GR

Funding

RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/L021633/1
6 · The paper itself

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that play a key role in the oxidative degradation of various biopolymers such as cellulose and chitin. While hunting for new LPMOs, we identified a new family of proteins, defined here as X325, in various fungal lineages. The three-dimensional structure of X325 revealed an overall LPMO fold and a His brace with an additional Asp ligand to Cu(II). Although LPMO-type activity of X325 members was initially expected, we demonstrated that X325 members do not perform oxidative cleavage of polysaccharides, establishing that X325s are not LPMOs. Investigations of the biological role of X325 in the ectomycorrhizal fungus Laccaria bicolor revealed exposure of the X325 protein at the interface between fungal hyphae and tree rootlet cells. Our results provide insights into a family of copper-containing proteins, which is widespread in the fungal kingdom and is evolutionarily related to LPMOs, but has diverged to biological functions other than polysaccharide degradation.

Indexed as

Binding SitesCelluloseChitinCopperFungal ProteinsFungiMixed Function OxygenasesOxidation-ReductionPhylogenyPolysaccharidesCelluloseChitinCopperFungal ProteinsMixed Function OxygenasesPolysaccharides

Identifiers

PMID31932718
OpenAlexW2999365647

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.