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Cited by 23Cellular transport and secretionAdvanced Electron Microscopy Techniques and ApplicationsATP Synthase and ATPases Research

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Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate

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Rüttermann, Maximilian, Koci, Michelle, Lill, Pascal, Geladas, Ermis Dionysios, Kaschani, Farnusch, Klink, Björn Udo, Erdmann, Ralf, Gatsogiannis, Christos·2023·Nature Communications
DOI 10.1038/s41467-023-41640-9PMC PMC10518020

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Abstract

The double-ring AAA+ ATPase Pex1/Pex6 is required for peroxisomal receptor recycling and is essential for peroxisome formation. Pex1/Pex6 mutations cause severe peroxisome associated developmental disorders. Despite its pathophysiological importance, mechanistic details of the heterohexamer are not yet available. Here, we report cryoEM structures of Pex1/Pex6 from Saccharomyces cerevisiae , with an endogenous protein substrate trapped in the central pore of the catalytically active second ring (D2). Pairs of Pex1/Pex6(D2) subdomains engage the substrate via a staircase of pore-1 loops with distinct properties. The first ring (D1) is catalytically inactive but undergoes significant conformational changes resulting in alternate widening and narrowing of its pore. These events are fueled by ATP hydrolysis in the D2 ring and disengagement of a “twin-seam” Pex1/Pex6(D2) heterodimer from the staircase. Mechanical forces are propagated in a unique manner along Pex1/Pex6 interfaces that are not available in homo-oligomeric AAA-ATPases. Our structural analysis reveals the mechanisms of how Pex1 and Pex6 coordinate to achieve substrate translocation.

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Metadata

Authors
Rüttermann, M., Koci, M., Lill, P., Geladas, E. D., Kaschani, F., Klink, B. U., Erdmann, R., & Gatsogiannis, C.
Affiliations
  • University of Münster (DE)
  • Max Planck Institute of Molecular Physiology (DE)
  • University of Duisburg-Essen (DE)
  • Ruhr University Bochum (DE)
Corresponding author
Gatsogiannis, Christos
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2023-09-23
Volume
14
Issue
1
Pages
5942-5942
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-023-41640-9
PMC
PMC10518020
OpenAlex
W4386980275
Cited by
23
References
1
Citations by year
2026: 10 · 2025: 10 · 2024: 2 · 2023: 1
FWCI
3.33
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • URN:NBN Resolver for Germany & Switzerland (German National Library) (submittedVersion, cc-by)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Universitäts- und Landesbibliothek Münster (cc-by)
Funders
Deutsche Forschungsgemeinschaft (SFB1430,SFB 1430 Project-ID 424228829, FOR 1905 (PerTrans consortium) GA 2519/1-2)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords
AAA+ ATPase, peroxisome biogenesis, heterohexamer, substrate translocation, Saccharomyces cerevisiae
MeSH terms
ATPases Associated with Diverse Cellular Activities, Proton-Translocating ATPases, Membrane Proteins, Mutation, Saccharomyces cerevisiae, Substrate Specificity, Cryoelectron Microscopy, Peroxisomes, Saccharomyces cerevisiae Proteins

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