Evidence map›Paper›PMID 26151670›Full record

ArticleNature communications2015

Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation.

Tien-Chye Tan, Daniel Kracher, Rosaria Gandini, Christoph Sygmund, Roman Kittl, Dietmar Haltrich, B Martin Hällberg, Roland Ludwig, Christina Divne

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
38.3field-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

104 citing papers in PubMed, 249 citations in OpenAlex.

  1. Article
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  3. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
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  11. Article
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  14. Discovery of a Novel Cellobiose Dehydrogenase fromJournal of microbiology and biotechnology · 2024
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Interface engineering of cellobiose dehydrogenase improves interdomain electron transfer.Protein science : a publication of the Protein Society · 2023
    Article
  20. Article

44 more citing papers are in PubMed but not listed here.

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.

Tien-Chye Tan1] School of Biotechnology, KTH Royal Institute of Technology, AlbaNova University Center, Roslagstullsbacken 21, Stockholm S-10691, Sweden [2] Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheelelaboratoriet, Scheeles väg 2, Stockholm S-17177, Sweden.
Daniel KracherFood Biotechnology Laboratory, Department of Food Science and Technology, Vienna Institute of Biotechnology (VIBT), BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, Vienna A-1190, Austria.
Rosaria Gandini1] School of Biotechnology, KTH Royal Institute of Technology, AlbaNova University Center, Roslagstullsbacken 21, Stockholm S-10691, Sweden [2] Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheelelaboratoriet, Scheeles väg 2, Stockholm S-17177, Sweden.
Christoph SygmundFood Biotechnology Laboratory, Department of Food Science and Technology, Vienna Institute of Biotechnology (VIBT), BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, Vienna A-1190, Austria.
Roman KittlFood Biotechnology Laboratory, Department of Food Science and Technology, Vienna Institute of Biotechnology (VIBT), BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, Vienna A-1190, Austria.
Dietmar HaltrichFood Biotechnology Laboratory, Department of Food Science and Technology, Vienna Institute of Biotechnology (VIBT), BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, Vienna A-1190, Austria.
B Martin Hällberg1] Department of Cell and Molecular Biology, Karolinska Institutet, Stockholm S-17177, Sweden [2] European Molecular Biology Laboratory, Hamburg Unit, Hamburg 22603, Germany; and Centre for Structural Systems Biology (CSSB), DESY-Campus, Hamburg 22603, Germany.
Roland LudwigFood Biotechnology Laboratory, Department of Food Science and Technology, Vienna Institute of Biotechnology (VIBT), BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, Vienna A-1190, Austria.
Christina Divne1] School of Biotechnology, KTH Royal Institute of Technology, AlbaNova University Center, Roslagstullsbacken 21, Stockholm S-10691, Sweden [2] Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheelelaboratoriet, Scheeles väg 2, Stockholm S-17177, Sweden.
BOKU University · ATKarolinska Institutet · SEEuropean Molecular Biology Laboratory · DEKTH Royal Institute of Technology · SE

Funding

MINOS (Macromolecular Insights on Nucleic acids Optimized by Scattering)R01GM105404 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 2012 to 2015
$2.1M
Austrian Science Fund FWF P 25148Austrian Science Fund FWF W 1224NIGMS NIH HHS R01 GM105404NIGMS NIH HHS R01GM105404
6 · The paper itself

Abstract

A new paradigm for cellulose depolymerization by fungi focuses on an oxidative mechanism involving cellobiose dehydrogenases (CDH) and copper-dependent lytic polysaccharide monooxygenases (LPMO); however, mechanistic studies have been hampered by the lack of structural information regarding CDH. CDH contains a haem-binding cytochrome (CYT) connected via a flexible linker to a flavin-dependent dehydrogenase (DH). Electrons are generated from cellobiose oxidation catalysed by DH and shuttled via CYT to LPMO. Here we present structural analyses that provide a comprehensive picture of CDH conformers, which govern the electron transfer between redox centres. Using structure-based site-directed mutagenesis, rapid kinetics analysis and molecular docking, we demonstrate that flavin-to-haem interdomain electron transfer (IET) is enabled by a haem propionate group and that rapid IET requires a closed CDH state in which the propionate is tightly enfolded by DH. Following haem reduction, CYT reduces LPMO to initiate oxygen activation at the copper centre and subsequent cellulose depolymerization.

Indexed as

Carbohydrate ConformationCarbohydrate DehydrogenasesCatalytic DomainCelluloseCloning, MolecularFlavin-Adenine DinucleotideFungal ProteinsFungiHemeModels, MolecularMutagenesis, Site-DirectedMutationProtein BindingProtein ConformationCarbohydrate Dehydrogenasescellobiose-quinone oxidoreductaseCelluloseFlavin-Adenine DinucleotideFungal ProteinsHeme

Identifiers

PMID26151670
PMCPMC4507011
OpenAlexW791576560

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.