Evidence map›Paper›PMID 27458710›Full record

ArticlePloS one2016

Structure of Alcohol Oxidase from Pichia pastoris by Cryo-Electron Microscopy.

Janet Vonck, David N Parcej, Deryck J Mills

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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Review
  3. Chemical reviews · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Engineering the methylotrophic yeastFrontiers in bioengineering and biotechnology · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Multiplicity of enzymatic functions in the CAZy AA3 family.Applied microbiology and biotechnology · 2018
    Review
  17. Article
  18. Article
  19. Trends in the Electron Microscopy Data Bank (EMDB).Acta crystallographica. Section D, Structural biology · 2017
    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

3 authors at 1 institution in 1 country.

Janet VonckDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
David N ParcejDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Deryck J MillsDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Max Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The first step in methanol metabolism in methylotrophic yeasts, the oxidation of methanol and higher alcohols with molecular oxygen to formaldehyde and hydrogen peroxide, is catalysed by alcohol oxidase (AOX), a 600-kDa homo-octamer containing eight FAD cofactors. When these yeasts are grown with methanol as the carbon source, AOX forms large crystalline arrays in peroxisomes. We determined the structure of AOX by cryo-electron microscopy at a resolution of 3.4 Å. All residues of the 662-amino acid polypeptide as well as the FAD are well resolved. AOX shows high structural homology to other members of the GMC family of oxidoreductases, which share a conserved FAD binding domain, but have different substrate specificities. The preference of AOX for small alcohols is explained by the presence of conserved bulky aromatic residues near the active site. Compared to the other GMC enzymes, AOX contains a large number of amino acid inserts, the longest being 75 residues. These segments are found at the periphery of the monomer and make extensive inter-subunit contacts which are responsible for the very stable octamer. A short surface helix forms contacts between two octamers, explaining the tendency of AOX to form crystals in the peroxisomes.

Indexed as

Cryoelectron MicroscopyAlcohol OxidoreductasesCatalytic DomainFlavin-Adenine DinucleotideModels, MolecularPichiaProtein BindingProtein ConformationProtein Interaction Domains and MotifsStructure-Activity RelationshipSubstrate Specificityalcohol oxidaseAlcohol OxidoreductasesFlavin-Adenine Dinucleotide

Identifiers

PMID27458710
PMCPMC4961394
OpenAlexW2498142038

What OpenQuestion holds

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LicenceCC BY
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.