Evidence map›Paper›PMID 26905908›Full record

ArticlePloS one2016

Crystal Structure of Alcohol Oxidase from Pichia pastoris.

Christian Koch, Piotr Neumann, Oliver Valerius, Ivo Feussner, Ralf Ficner

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Novel Basidiomycetous Alcohol Oxidase fromInternational journal of molecular sciences · 2024
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.Microbiology and molecular biology reviews : MMBR · 2018
    Review
  16. Article
  17. Multiplicity of enzymatic functions in the CAZy AA3 family.Applied microbiology and biotechnology · 2018
    Review
  18. Article
  19. 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

5 authors at 1 institution in 1 country.

Christian KochDepartment of Plant Biochemistry, Albrecht-von-Haller-Institute, Georg-August-University Goettingen, Justus-von-Liebig-Weg 11, 37077, Goettingen, Germany.
Piotr NeumannDepartment of Molecular Structural Biology, Institute of Microbiology und Genetics, Georg-August-University, Justus-von-Liebig-Weg 11, 37077, Goettingen, Germany.
Oliver ValeriusDepartment of Molecular Microbiology and Genetics, Institute for Microbiology und Genetics, Georg-August-University, Griesebachstr. 8, 37077, Goettingen, Germany.
Ivo FeussnerDepartment of Plant Biochemistry, Albrecht-von-Haller-Institute, Georg-August-University Goettingen, Justus-von-Liebig-Weg 11, 37077, Goettingen, Germany.
Ralf FicnerDepartment of Molecular Structural Biology, Institute of Microbiology und Genetics, Georg-August-University, Justus-von-Liebig-Weg 11, 37077, Goettingen, Germany.
University of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FAD-dependent alcohol oxidases (AOX) are key enzymes of methylotrophic organisms that can utilize lower primary alcohols as sole source of carbon and energy. Here we report the crystal structure analysis of the methanol oxidase AOX1 from Pichia pastoris. The crystallographic phase problem was solved by means of Molecular Replacement in combination with initial structure rebuilding using Rosetta model completion and relaxation against an averaged electron density map. The subunit arrangement of the homo-octameric AOX1 differs from that of octameric vanillyl alcohol oxidase and other dimeric or tetrameric alcohol oxidases, due to the insertion of two large protruding loop regions and an additional C-terminal extension in AOX1. In comparison to other alcohol oxidases, the active site cavity of AOX1 is significantly reduced in size, which could explain the observed preference for methanol as substrate. All AOX1 subunits of the structure reported here harbor a modified flavin adenine dinucleotide, which contains an arabityl chain instead of a ribityl chain attached to the isoalloxazine ring.

Indexed as

Alcohol OxidoreductasesCrystallography, X-RayFlavin-Adenine DinucleotideFungal ProteinsPichiaProtein Structure, QuaternaryProtein Structure, Tertiaryalcohol oxidaseAlcohol OxidoreductasesFlavin-Adenine DinucleotideFungal Proteins

Identifiers

PMID26905908
PMCPMC4764120
OpenAlexW2281626582

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.