Evidence map›Paper›PMID 26308900›Full record

ArticleNature2015

A four-helix bundle stores copper for methane oxidation.

Nicolas Vita, Semeli Platsaki, Arnaud Baslé, Stephen J Allen, Neil G Paterson, Andrew T Crombie, J Colin Murrell, Kevin J Waldron, Christopher Dennison

Open access · greenAbstract read
In one paragraph

Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
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  11. Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  12. Review
  13. Copper delivery to an endospore coat protein ofFrontiers in cell and developmental biology · 2022
    Article
  14. Article
  15. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 5 institutions in 2 countries.

Nicolas VitaInstitute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Semeli PlatsakiInstitute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Arnaud BasléInstitute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Stephen J AllenInstitute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Neil G PatersonDiamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK.
Andrew T CrombieSchool of Environmental Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.
J Colin MurrellSchool of Environmental Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.
Kevin J WaldronInstitute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Christopher DennisonInstitute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Newcastle University · GBDiamond Light Source · GBNorthwestern University · USNorwich Research Park · GBUniversity of East Anglia · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F012713/1Biotechnology and Biological Sciences Research Council BB/K008439/1Wellcome Trust 098375Wellcome Trust 098375/Z/12/Z
6 · The paper itself

Abstract

Methane-oxidizing bacteria (methanotrophs) require large quantities of copper for the membrane-bound (particulate) methane monooxygenase. Certain methanotrophs are also able to switch to using the iron-containing soluble methane monooxygenase to catalyse methane oxidation, with this switchover regulated by copper. Methane monooxygenases are nature's primary biological mechanism for suppressing atmospheric levels of methane, a potent greenhouse gas. Furthermore, methanotrophs and methane monooxygenases have enormous potential in bioremediation and for biotransformations producing bulk and fine chemicals, and in bioenergy, particularly considering increased methane availability from renewable sources and hydraulic fracturing of shale rock. Here we discover and characterize a novel copper storage protein (Csp1) from the methanotroph Methylosinus trichosporium OB3b that is exported from the cytosol, and stores copper for particulate methane monooxygenase. Csp1 is a tetramer of four-helix bundles with each monomer binding up to 13 Cu(I) ions in a previously unseen manner via mainly Cys residues that point into the core of the bundle. Csp1 is the first example of a protein that stores a metal within an established protein-folding motif. This work provides a detailed insight into how methanotrophs accumulate copper for the oxidation of methane. Understanding this process is essential if the wide-ranging biotechnological applications of methanotrophs are to be realized. Cytosolic homologues of Csp1 are present in diverse bacteria, thus challenging the dogma that such organisms do not use copper in this location.

Indexed as

Amino Acid MotifsBacterial ProteinsCopperCrystallography, X-RayCytosolMethaneMethylosinus trichosporiumModels, MolecularOxidation-ReductionOxygenasesProtein FoldingProtein Structure, SecondaryBacterial ProteinsCopperMethanemethane monooxygenaseOxygenases

Identifiers

PMID26308900
PMCPMC4561512
OpenAlexW2155454872

What OpenQuestion holds

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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.