Evidence map›Paper›PMID 29097656›Full record

ArticleNature communications2017

Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex.

Michal T Boniecki, Sven A Freibert, Ulrich Mühlenhoff, Roland Lill, Miroslaw Cygler

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
5.9field-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

117 citing papers in PubMed, 234 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Regulation of mitochondrial iron homeostasis in tumor cells.Molecular medicine (Cambridge, Mass.) · 2026
    Review
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  9. Article
  10. Review
  11. Mitochondrial medicine in obesity: a scoping review.Open medicine (Warsaw, Poland) · 2026
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

57 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 2 institutions in 2 countries.

Michal T BonieckiDepartment of Biochemistry, University of Saskatchewan, 107 Wiggins Road, Saskatoon, SK, Canada, S7N 5E5.
Sven A FreibertInstitut für Zytobiologie und Zytopathologie, Philipps-Universität, Robert-Koch-Strasse 6, 35032, Marburg, Germany.ORCID http://orcid.org/0000-0002-8521-2963
Ulrich MühlenhoffInstitut für Zytobiologie und Zytopathologie, Philipps-Universität, Robert-Koch-Strasse 6, 35032, Marburg, Germany.
Roland LillInstitut für Zytobiologie und Zytopathologie, Philipps-Universität, Robert-Koch-Strasse 6, 35032, Marburg, Germany. Lill@staff.uni-marburg.de.ORCID http://orcid.org/0000-0002-8345-6518
Miroslaw CyglerDepartment of Biochemistry, University of Saskatchewan, 107 Wiggins Road, Saskatoon, SK, Canada, S7N 5E5. Miroslaw.cygler@usask.ca.ORCID http://orcid.org/0000-0003-4579-1881
University of Saskatchewan · CAPhilipps University of Marburg · DE

Funding

CIHR MOP-48370
6 · The paper itself

Abstract

Iron-sulfur (Fe/S) clusters are essential protein cofactors crucial for many cellular functions including DNA maintenance, protein translation, and energy conversion. De novo Fe/S cluster synthesis occurs on the mitochondrial scaffold protein ISCU and requires cysteine desulfurase NFS1, ferredoxin, frataxin, and the small factors ISD11 and ACP (acyl carrier protein). Both the mechanism of Fe/S cluster synthesis and function of ISD11-ACP are poorly understood. Here, we present crystal structures of three different NFS1-ISD11-ACP complexes with and without ISCU, and we use SAXS analyses to define the 3D architecture of the complete mitochondrial Fe/S cluster biosynthetic complex. Our structural and biochemical studies provide mechanistic insights into Fe/S cluster synthesis at the catalytic center defined by the active-site Cys of NFS1 and conserved Cys, Asp, and His residues of ISCU. We assign specific regulatory rather than catalytic roles to ISD11-ACP that link Fe/S cluster synthesis with mitochondrial lipid synthesis and cellular energy status.

Indexed as

Acyl Carrier ProteinAmino Acid SequenceAmino Acid SubstitutionCarbon-Sulfur LyasesChaetomiumCrystallography, X-RayFrataxinFungal ProteinsHumansIron-Binding ProteinsIron-Regulatory ProteinsIron-Sulfur ProteinsMitochondriaMitochondrial ProteinsModels, MolecularMolecular Dynamics SimulationAcyl Carrier ProteinCarbon-Sulfur LyasesFrataxinFungal ProteinsIron-Binding ProteinsIron-Regulatory ProteinsIron-Sulfur ProteinsISCU protein, humanIsd11 protein, S cerevisiaeLYRM4 protein, humanMitochondrial ProteinsMultiprotein ComplexesNFS1 protein, humanSaccharomyces cerevisiae Proteins

Identifiers

PMID29097656
PMCPMC5668364
OpenAlexW2765394645

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.