Evidence map›Paper›PMID 24317491›Full record

ArticleNature structural & molecular biology2014

Copper-transporting P-type ATPases use a unique ion-release pathway.

Magnus Andersson, Daniel Mattle, Oleg Sitsel, Tetyana Klymchuk, Anna Marie Nielsen, Lisbeth Birk Møller, Stephen H White, Poul Nissen, Pontus Gourdon

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

54 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Role of cuproptosis in digestive system tumors (Review).International journal of molecular medicine · 2026
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  6. In vitro reconstitution of transition metal transporters.The Journal of biological chemistry · 2024
    Review
  7. Article
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  9. Article
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  11. Article
  12. Article
  13. Article
  14. The NaThe Journal of biological chemistry · 2022
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021
    Review
  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

9 authors at 3 institutions in 2 countries.

Magnus Andersson1] Department of Physiology and Biophysics, University of California at Irvine, Irvine, California, USA. [2] [3].
Daniel Mattle1] Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark. [2] [3].
Oleg SitselCentre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Tetyana KlymchukCentre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Anna Marie NielsenCentre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Lisbeth Birk MøllerApplied Human Molecular Genetics, Kennedy Center, Copenhagen University Hospital, Rigshospitalet, Glostrup, Denmark.
Stephen H WhiteDepartment of Physiology and Biophysics, University of California at Irvine, Irvine, California, USA.ORCID 0000000185407907
Poul NissenCentre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.ORCID 0000000309486628
Pontus GourdonCentre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Danish National Research Foundation · DKUniversity of California, Irvine · USCopenhagen University Hospital · DK

Funding

Project 3: Structural Studies of Voltage-Gated Potassium Channels as FunctionP01GM086685 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WORCESTER, DAVID · 2009 to 2013
$6.7M
Membrane Protein Folding and AssemblyR01GM074637 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2006 to 2020
$4.5M
NIGMS NIH HHS GM074637NIGMS NIH HHS GM086685NIGMS NIH HHS P01 GM086685NIGMS NIH HHS R01 GM074637
6 · The paper itself

Abstract

Heavy metals in cells are typically regulated by PIB-type ATPases. The first structure of the class, a Cu(+)-ATPase from Legionella pneumophila (LpCopA), outlined a copper transport pathway across the membrane, which was inferred to be occluded. Here we show by molecular dynamics simulations that extracellular water solvated the transmembrane (TM) domain, results indicative of a Cu(+)-release pathway. Furthermore, a new LpCopA crystal structure determined at 2.8-Å resolution, trapped in the preceding E2P state, delineated the same passage, and site-directed-mutagenesis activity assays support a functional role for the conduit. The structural similarities between the TM domains of the two conformations suggest that Cu(+)-ATPases couple dephosphorylation and ion extrusion differently than do the well-characterized PII-type ATPases. The ion pathway explains why certain Menkes' and Wilson's disease mutations impair protein function and points to a site for inhibitors targeting pathogens.

Indexed as

Adenosine TriphosphatasesCopperIonsMolecular Dynamics SimulationMutagenesis, Site-DirectedProtein ConformationAdenosine TriphosphatasesCopperIons

Identifiers

PMID24317491
PMCPMC3904665
OpenAlexW2073224102

What OpenQuestion holds

Textmetadata
LicenceTDM
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.