Evidence map›Paper›PMID 27373333›Full record

ArticleMolecular cell2016

Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology.

Alexander Hahn, Kristian Parey, Maike Bublitz, Deryck J Mills, Volker Zickermann, Janet Vonck, Werner Kühlbrandt, Thomas Meier

Open access · hybridAbstract readVideo-Audio Media
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
20.2field-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

137 citing papers in PubMed, 267 citations in OpenAlex.

  1. Article
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  8. Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025
    Review
  9. In situ cryo-ET visualization of mitochondrial depolarization and mitophagic engulfment.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. bioRxiv : the preprint server for biology · 2025
    Article
  12. Article
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  17. Review
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  20. Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

77 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

8 authors at 2 institutions in 1 country.

Alexander HahnDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
Kristian PareyDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
Maike BublitzInstitute of Biochemistry, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany.
Deryck J MillsDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
Volker ZickermannInstitute of Biochemistry II, Medical School, Goethe University Frankfurt, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany.
Janet VonckDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
Werner KühlbrandtDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany. Electronic address: werner.kuehlbrandt@biophys.mpg.de.
Thomas MeierDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany. Electronic address: t.meier@imperial.ac.uk.
Max Planck Institute of Biophysics · DEGoethe University Frankfurt · DE

Funding

Wellcome TrustWellcome Trust WT110068/Z/15/Z
6 · The paper itself

Abstract

We determined the structure of a complete, dimeric F1Fo-ATP synthase from yeast Yarrowia lipolytica mitochondria by a combination of cryo-EM and X-ray crystallography. The final structure resolves 58 of the 60 dimer subunits. Horizontal helices of subunit a in Fo wrap around the c-ring rotor, and a total of six vertical helices assigned to subunits a, b, f, i, and 8 span the membrane. Subunit 8 (A6L in human) is an evolutionary derivative of the bacterial b subunit. On the lumenal membrane surface, subunit f establishes direct contact between the two monomers. Comparison with a cryo-EM map of the F1Fo monomer identifies subunits e and g at the lateral dimer interface. They do not form dimer contacts but enable dimer formation by inducing a strong membrane curvature of ∼100°. Our structure explains the structural basis of cristae formation in mitochondria, a landmark signature of eukaryotic cell morphology.

Indexed as

Adenosine TriphosphateCatalysisCryoelectron MicroscopyCrystallography, X-RayFungal ProteinsMitochondriaMitochondrial MembranesMitochondrial Proton-Translocating ATPasesModels, MolecularProtein Conformation, alpha-HelicalProtein MultimerizationProtein SubunitsStructure-Activity RelationshipYarrowiaAdenosine TriphosphateF1F0-ATP synthaseFungal ProteinsMitochondrial Proton-Translocating ATPasesProtein Subunitsbioenergeticscryoelectron microscopyF(1)F(o)-ATP synthase dimerinner membrane morphologymembrane protein complexmitochondriarotary ATPase mechanismX-ray crystallographyyeast Yarrowia lipolytica

Identifiers

PMID27373333
PMCPMC4980432
OpenAlexW2465554358

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.