Evidence map›Paper›PMID 34762655›Full record

ArticlePLoS biology2021

Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.

Satya Prathyusha Bhamidimarri, Tessa R Young, Muralidharan Shanmugam, Sandra Soderholm, Arnaud Baslé, Dirk Bumann, Bert van den Berg

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

27 citing papers in PubMed, 35 citations in OpenAlex.

  1. Targeting Outer Membrane Vesicles ofJournal of microbiology and biotechnology · 2026
    Review
  2. Review
  3. Identification of iron and zinc responsive TonB-dependent transporters in Pseudomonas aeruginosa.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Article
  4. Article
  5. CuiT is a Cu importer required for metal homeostasis inBiochemistry and biophysics reports · 2026
    Article
  6. Article
  7. Review
  8. CrpH ofFrontiers in microbiology · 2026
    Article
  9. Article
  10. Regulatory Characterization of Two Cop Systems for Copper Resistance inInternational journal of molecular sciences · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. CuBiomolecules · 2023
    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

7 authors at 4 institutions in 2 countries.

Satya Prathyusha BhamidimarriBiosciences Institute, The Medical School, Newcastle University, Newcastle upon Tyne, United Kingdom.ORCID 0000-0002-6704-3385
Tessa R YoungDepartment of Biosciences, Durham University, United Kingdom.
Muralidharan ShanmugamPhoton Science Institute and Manchester Institute of Biotechnology, University of Manchester, Oxford Road, United Kingdom.ORCID 0000-0003-3818-1401
Sandra SoderholmFocal Area Infection Biology, University of Basel, Basel, Switzerland.
Arnaud BasléBiosciences Institute, The Medical School, Newcastle University, Newcastle upon Tyne, United Kingdom.
Dirk BumannFocal Area Infection Biology, University of Basel, Basel, Switzerland.
Bert van den BergBiosciences Institute, The Medical School, Newcastle University, Newcastle upon Tyne, United Kingdom.ORCID 0000-0003-1966-8804
Newcastle University · GBUniversity of Basel · CHDurham University · GBUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L009226/1Biotechnology and Biological Sciences Research Council BB/R004366/1
6 · The paper itself

Abstract

Copper, while toxic in excess, is an essential micronutrient in all kingdoms of life due to its essential role in the structure and function of many proteins. Proteins mediating ionic copper import have been characterised in detail for eukaryotes, but much less so for prokaryotes. In particular, it is still unclear whether and how gram-negative bacteria acquire ionic copper. Here, we show that Pseudomonas aeruginosa OprC is an outer membrane, TonB-dependent transporter that is conserved in many Proteobacteria and which mediates acquisition of both reduced and oxidised ionic copper via an unprecedented CxxxM-HxM metal binding site. Crystal structures of wild-type and mutant OprC variants with silver and copper suggest that acquisition of Cu(I) occurs via a surface-exposed "methionine track" leading towards the principal metal binding site. Together with whole-cell copper quantitation and quantitative proteomics in a murine lung infection model, our data identify OprC as an abundant component of bacterial copper biology that may enable copper acquisition under a wide range of conditions.

Indexed as

AnimalsBacterial Outer Membrane ProteinsBinding SitesCopperIonsMaleMethionineMiceModels, MolecularProtein ConformationPseudomonas aeruginosaPseudomonas InfectionsBacterial Outer Membrane ProteinsCopperIonsMethionine

Identifiers

PMID34762655
PMCPMC8610252
OpenAlexW3213071751

What OpenQuestion holds

Textmetadata
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.