Evidence map›Paper›PMID 25326704›Full record

ArticleNature structural & molecular biology2014

Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport.

Ines A Ehrnstorfer, Eric R Geertsma, Els Pardon, Jan Steyaert, Raimund Dutzler

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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 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
13.1field-weighted citation impact, top 1% 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

108 citing papers in PubMed, 217 citations in OpenAlex.

  1. Review
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  3. Article
  4. Article
  5. Determinants of metal import and specificity in a bacterial transporter.bioRxiv : the preprint server for biology · 2026
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  11. Review
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  13. Identification of a divalent metal transporter required for cellular iron metabolism in malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Article
  16. Review
  17. Clinical microbiology reviews · 2024
    Review
  18. In vitro reconstitution of transition metal transporters.The Journal of biological chemistry · 2024
    Review
  19. Article
  20. Article

48 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 3 countries.

Ines A EhrnstorferDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Eric R GeertsmaDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Els Pardon1] Structural Biology Research Center, Vlaams Instituut voor Biotechnologie (VIB), Brussels, Belgium. [2] Structural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.
Jan Steyaert1] Structural Biology Research Center, Vlaams Instituut voor Biotechnologie (VIB), Brussels, Belgium. [2] Structural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.
Raimund DutzlerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
University of Zurich · CHGoethe University Frankfurt · DEVlaams Instituut voor Biotechnologie · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the SLC11 (NRAMP) family transport iron and other transition-metal ions across cellular membranes. These membrane proteins are present in all kingdoms of life with a high degree of sequence conservation. To gain insight into the determinants of ion selectivity, we have determined the crystal structure of Staphylococcus capitis DMT (ScaDMT), a close prokaryotic homolog of the family. ScaDMT shows a familiar architecture that was previously identified in the amino acid permease LeuT. The protein adopts an inward-facing conformation with a substrate-binding site located in the center of the transporter. This site is composed of conserved residues, which coordinate Mn2+, Fe2+ and Cd2+ but not Ca2+. Mutations of interacting residues affect ion binding and transport in both ScaDMT and human DMT1. Our study thus reveals a conserved mechanism for transition-metal ion selectivity within the SLC11 family.

Indexed as

Amino Acid SequenceAmino Acid Transport SystemsBacterial ProteinsBinding SitesCadmiumCations, DivalentCation Transport ProteinsConserved SequenceCrystallography, X-RayEscherichia coliGene ExpressionHumansIon TransportIronManganeseModels, MolecularAmino Acid Transport SystemsBacterial ProteinsCadmiumCations, DivalentCation Transport ProteinsDMRT1 proteinIronManganeseNatural Resistance-associated Macrophage Protein 1Recombinant ProteinsTranscription Factors

Identifiers

PMID25326704
OpenAlexW1992032455

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Registered trials

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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.