Evidence map›Paper›PMID 24064212›Full record

ArticleThe Journal of biological chemistry2013

Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (GH3) β-glucosidase structure and function.

Marisa A Lima, Mario Oliveira-Neto, Marco Antonio S Kadowaki, Flavio R Rosseto, Erica T Prates, Fabio M Squina, Adriana F P Leme, Munir S Skaf, Igor Polikarpov

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.2field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Whole-Genome Resequencing ofInternational journal of molecular sciences · 2026
    Article
  4. Identification of Laccase Family ofInternational journal of molecular sciences · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Production of a β-Glucosidase-Rich Cocktail fromJournal of fungi (Basel, Switzerland) · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Crystal Structure of a GH3 β-Glucosidase from the Thermophilic FungusInternational journal of molecular sciences · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  20. Article
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 5 institutions in 1 country.

Marisa A LimaFrom the Instituto de Física de São Carlos, Universidade de São Paulo, Caixa Postal 369, São Carlos 13560-970, SP.
Mario Oliveira-Neto
Marco Antonio S Kadowaki
Flavio R Rosseto
Erica T Prates
Fabio M Squina
Adriana F P Leme
Munir S Skaf
Igor Polikarpov
Universidade de São Paulo · BRUniversidade Estadual Paulista (Unesp) · BRBrazilian Biosciences National Laboratory · BRLaboratório Nacional de Ciência e Tecnologia do Bioetanol · BRUniversidade Estadual de Campinas (UNICAMP) · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aspergillus niger is known to secrete large amounts of β-glucosidases, which have a variety of biotechnological and industrial applications. Here, we purified an A. niger β-glucosidase (AnBgl1) and conducted its biochemical and biophysical analyses. Purified enzyme with an apparent molecular mass of 116 kDa forms monomers in solution as judged by native gel electrophoresis and has a pI value of 4.55, as found for most of the fungi of β-glucosidases. Surprisingly, the small angle x-ray experiments reveal that AnBgl1 has a tadpole-like structure, with the N-terminal catalytic domain and C-terminal fibronectin III-like domain (FnIII) connected by the long linker peptide (∼100 amino acid residues) in an extended conformation. This molecular organization resembles the one adopted by other cellulases (such as cellobiohydrolases, for example) that frequently contain a catalytic domain linked to the cellulose-binding module that mediates their binding to insoluble and polymeric cellulose. The reasons why AnBgl1, which acts on the small soluble substrates, has a tadpole molecular shape are not entirely clear. However, our enzyme pulldown assays with different polymeric substrates suggest that AnBgl1 has little or no capacity to bind to and to adsorb cellulose, xylan, and starch, but it has high affinity to lignin. Molecular dynamics simulations suggested that clusters of residues located in the C-terminal FnIII domain interact strongly with lignin fragments. The simulations showed that numerous arginine residues scattered throughout the FnIII surface play an important role in the interaction with lignin by means of cation-π stacking with the lignin aromatic rings. These results indicate that the C-terminal FnIII domain could be operational for immobilization of the enzyme on the cell wall and for the prevention of unproductive binding of cellulase to the biomass lignin.

Indexed as

Aspergillus nigerCelluloseCell WallFungal ProteinsGlucan 1,3-beta-GlucosidaseLigninProtein BindingProtein Structure, TertiaryStarchStructure-Activity RelationshipSubstrate SpecificityXylansCelluloseFungal ProteinsGlucan 1,3-beta-GlucosidaseLigninStarchXylansAspergillus nigerEnzyme MechanismsEnzymesEnzyme StructureFungiGlycobiologyGlycoside Hydrolase Family 3Multidomain ProteinsSAXSβ-Glucosidase

Identifiers

PMID24064212
PMCPMC3829149
OpenAlexW2056526417

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.