Evidence map›Paper›PMID 26257399›Full record

ArticleProtein science : a publication of the Protein Society2015

The structure of the Caenorhabditis elegans manganese superoxide dismutase MnSOD-3-azide complex.

Gary J Hunter, Chi H Trinh, Rosalin Bonetta, Emma E Stewart, Diane E Cabelli, Therese Hunter

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. The curious life of human mitochondrial SOD2.International journal of biological macromolecules · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Redox manipulation of the manganese metal in human manganese superoxide dismutase for neutron diffraction.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  8. Article
  9. The first crystal structure of manganese superoxide dismutase from the genus Staphylococcus.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  10. Review
  11. Article
  12. 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

6 authors.

Gary J HunterDepartment of Physiology and Biochemistry, Faculty of Medicine and Surgery, University of Malta, Msida, Malta.
Chi H TrinhAstbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Rosalin BonettaDepartment of Physiology and Biochemistry, Faculty of Medicine and Surgery, University of Malta, Msida, Malta.
Emma E StewartAstbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Diane E CabelliChemistry Department, Brookhaven National Laboratory, Upton, New York.
Therese HunterDepartment of Physiology and Biochemistry, Faculty of Medicine and Surgery, University of Malta, Msida, Malta.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

C. elegans MnSOD-3 has been implicated in the longevity pathway and its mechanism of catalysis is relevant to the aging process and carcinogenesis. The structures of MnSOD-3 provide unique crystallographic evidence of a dynamic region of the tetrameric interface (residues 41-54). We have determined the structure of the MnSOD-3-azide complex to 1.77-Å resolution. Analysis of this complex shows that the substrate analog, azide, binds end-on to the manganese center as a sixth ligand and that it ligates directly to a third and new solvent molecule also positioned within interacting distance to the His30 and Tyr34 residues of the substrate access funnel. This is the first structure of a eukaryotic MnSOD-azide complex that demonstrates the extended, uninterrupted hydrogen-bonded network that forms a proton relay incorporating three outer sphere solvent molecules, the substrate analog, the gateway residues, Gln142, and the solvent ligand. This configuration supports the formation and release of the hydrogen peroxide product in agreement with the 5-6-5 catalytic mechanism for MnSOD. The high product dissociation constant k4 of MnSOD-3 reflects low product inhibition making this enzyme efficient even at high levels of superoxide.

Indexed as

AzidesCaenorhabditis elegans ProteinsHistidineModels, MolecularProtein ConformationSuperoxide DismutaseAzidesCaenorhabditis elegans ProteinsHistidineSod-3 protein, C elegansSuperoxide Dismutasecatalytic mechanismconformational variationMnSOD-3-azide complexproduct inhibitionsuperoxide dismutase

Identifiers

PMID26257399
PMCPMC4622211

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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.