Evidence map›Paper›PMID 26472926›Full record

ArticleThe Journal of biological chemistry2015

Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis.

Kei Hirabayashi, Eiki Yuda, Naoyuki Tanaka, Sumie Katayama, Kenji Iwasaki, Takashi Matsumoto, Genji Kurisu, F Wayne Outten, Keiichi Fukuyama, Yasuhiro Takahashi and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

40 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Review
  3. The structure of the SufBCbioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Recent Characterization of Key Proteins to Combat Tuberculosis.Advances in experimental medicine and biology · 2026
    Review
  6. A minimal SufBMicrobiology spectrum · 2025
    Article
  7. SmsB-SmsC machinery inApplied and environmental microbiology · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Genome mining ofFrontiers in microbiology · 2024
    Article
  13. The Benefits of Toxicity:Microorganisms · 2023
    Article
  14. Review
  15. TheeLife · 2023
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  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

11 authors at 6 institutions in 2 countries.

Kei HirabayashiFrom the Department of Biological Sciences, Graduate School of Science, Osaka University, Osaka 560-0043, Japan, the Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki 889-1692, Japan.
Eiki Yudathe Division of Life Science, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan.
Naoyuki Tanakathe Division of Life Science, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan.
Sumie Katayamathe Institute for Protein Research, Osaka University, Osaka 565-0871, Japan.
Kenji Iwasakithe Institute for Protein Research, Osaka University, Osaka 565-0871, Japan.
Takashi Matsumotothe Rigaku Corporation, Tokyo 196-8666, Japan.
Genji Kurisuthe Institute for Protein Research, Osaka University, Osaka 565-0871, Japan.
F Wayne Outtenthe Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, and.
Keiichi Fukuyamathe Division of Applied Chemistry, Graduate School of Engineering Osaka University, Osaka 565-0871, Japan.
Yasuhiro Takahashithe Division of Life Science, Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan, ytaka@molbiol.saitama-u.ac.jp.
Kei Wadathe Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki 889-1692, Japan, keiwada@med.miyazaki-u.ac.jp.
Osaka University · JPSaitama University · JPProtein Research Foundation · JPRigaku (Japan) · JPUniversity of Miyazaki · JPUniversity of South Carolina · US

Funding

Conformational dynamics and allosteric regulation during stress-responsive metallocofactor assemblyR01GM112919 · NIGMS · UNIVERSITY OF ALABAMA IN TUSCALOOSA · PI Patrick Frantom · 2015 to 2026
$2.8M
Characterization of the Suf Fe-S Cluster Biosynthesis Pathway Under StressR01GM081706 · NIGMS · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI OUTTEN, FRANKLIN WAYNE · 2007 to 2011
$1.1M
NIGMS NIH HHS GM 112919NIGMS NIH HHS GM 81706NIGMS NIH HHS R01 GM081706NIGMS NIH HHS R01 GM112919
6 · The paper itself

Abstract

ATP-binding cassette (ABC)-type ATPases are chemomechanical engines involved in diverse biological pathways. Recent genomic information reveals that ABC ATPase domains/subunits act not only in ABC transporters and structural maintenance of chromosome proteins, but also in iron-sulfur (Fe-S) cluster biogenesis. A novel type of ABC protein, the SufBCD complex, functions in the biosynthesis of nascent Fe-S clusters in almost all Eubacteria and Archaea, as well as eukaryotic chloroplasts. In this study, we determined the first crystal structure of the Escherichia coli SufBCD complex, which exhibits the common architecture of ABC proteins: two ABC ATPase components (SufC) with function-specific components (SufB-SufD protomers). Biochemical and physiological analyses based on this structure provided critical insights into Fe-S cluster assembly and revealed a dynamic conformational change driven by ABC ATPase activity. We propose a molecular mechanism for the biogenesis of the Fe-S cluster in the SufBCD complex.

Indexed as

Amino Acid SequenceATP-Binding Cassette TransportersEscherichia coliEscherichia coli ProteinsIron-Sulfur ProteinsModels, MolecularMolecular Sequence DataScattering, Small AngleSequence Homology, Amino AcidX-Ray DiffractionATP-Binding Cassette TransportersEscherichia coli ProteinsIron-Sulfur ProteinsABC ATPaseABC transporterATPaseconformational changeiron-sulfur proteinSuf machineryx-ray crystallography

Identifiers

PMID26472926
PMCPMC4705970
OpenAlexW2195872026

What OpenQuestion holds

Textmetadata
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.