Evidence map›Paper›PMID 35896548›Full record

ArticleNature communications2022

Structures of Atm1 provide insight into [2Fe-2S] cluster export from mitochondria.

Ping Li, Amber L Hendricks, Yong Wang, Rhiza Lyne E Villones, Karin Lindkvist-Petersson, Gabriele Meloni, J A Cowan, Kaituo Wang, Pontus Gourdon

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

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  16. Mitochondria function in cytoplasmic FeS protein biogenesis.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  17. Article
  18. Requirements for the biogenesis of [2Fe-2S] proteins in the human and yeast cytosol.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. 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 5 institutions in 4 countries.

Ping LiDepartment of Experimental Medical Science, Lund University, Sölvegatan 19, SE-221 84, Lund, Sweden.
Amber L HendricksDepartment of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH, 43210, USA.
Yong WangInstitute of Quantitative Biology, College of Life Sciences, Zhejiang University, Hangzhou, 310027, China.
Rhiza Lyne E VillonesDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W Campbell Rd., Richardson, TX, 75080, USA.
Karin Lindkvist-PeterssonDepartment of Experimental Medical Science, Lund University, Sölvegatan 19, SE-221 84, Lund, Sweden.ORCID 0000-0002-5209-3160
Gabriele MeloniDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W Campbell Rd., Richardson, TX, 75080, USA.ORCID 0000-0003-4976-1401
J A CowanDepartment of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH, 43210, USA.
Kaituo WangDepartment of Biomedical Sciences, Copenhagen University, Maersk Tower 7-9, Nørre Allé 14, DK-2200, Copenhagen N, Denmark. kaituo@sund.ku.dk.ORCID 0000-0002-5922-7109
Pontus GourdonDepartment of Experimental Medical Science, Lund University, Sölvegatan 19, SE-221 84, Lund, Sweden. pontus.gourdon@med.lu.se.ORCID 0000-0002-8631-3539
Lund University · SEThe Ohio State University · USThe University of Texas at Dallas · USUniversity of Copenhagen · DKChina International Science and Technology Cooperation · CN

Funding

Principles of selectivity and translocation in transition metal transporters, metallochaperones, and associated metalloproteinsR35GM128704 · NIGMS · UNIVERSITY OF TEXAS DALLAS · PI Gabriele Meloni · 2018 to 2026
$3.5M
NIGMS NIH HHS R35 GM128704
6 · The paper itself

Abstract

In eukaryotes, iron-sulfur clusters are essential cofactors for numerous physiological processes, but these clusters are primarily biosynthesized in mitochondria. Previous studies suggest mitochondrial ABCB7-type exporters are involved in maturation of cytosolic iron-sulfur proteins. However, the molecular mechanism for how the ABCB7-type exporters participate in this process remains elusive. Here, we report a series of cryo-electron microscopy structures of a eukaryotic homolog of human ABCB7, CtAtm1, determined at average resolutions ranging from 2.8 to 3.2 Å, complemented by functional characterization and molecular docking in silico. We propose that CtAtm1 accepts delivery from glutathione-complexed iron-sulfur clusters. A partially occluded state links cargo-binding to residues at the mitochondrial matrix interface that line a positively charged cavity, while the binding region becomes internalized and is partially divided in an early occluded state. Collectively, our findings substantially increase the understanding of the transport mechanism of eukaryotic ABCB7-type proteins.

Indexed as

Iron-Sulfur ProteinsMitochondrial ProteinsATP-Binding Cassette TransportersCryoelectron MicroscopyHumansIronMitochondriaMolecular Docking SimulationSulfurATP-Binding Cassette TransportersIronIron-Sulfur ProteinsMitochondrial ProteinsSulfur

Identifiers

PMID35896548
PMCPMC9329353
OpenAlexW4288723752

What OpenQuestion holds

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LicenceCC BY
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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.