IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v6y2015i1d10.1038_ncomms8331.html
   My bibliography  Save this article

Molecular snapshots of the Pex1/6 AAA+ complex in action

Author

Listed:
  • Susanne Ciniawsky

    (Gene Center Munich, Ludwig-Maximilians-Universität München)

  • Immanuel Grimm

    (Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, Ruhr-Universität Bochum)

  • Delia Saffian

    (Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, Ruhr-Universität Bochum)

  • Wolfgang Girzalsky

    (Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, Ruhr-Universität Bochum)

  • Ralf Erdmann

    (Institute of Biochemistry and Pathobiochemistry, Faculty of Medicine, Ruhr-Universität Bochum)

  • Petra Wendler

    (Gene Center Munich, Ludwig-Maximilians-Universität München)

Abstract

The peroxisomal proteins Pex1 and Pex6 form a heterohexameric type II AAA+ ATPase complex, which fuels essential protein transport across peroxisomal membranes. Mutations in either ATPase in humans can lead to severe peroxisomal disorders and early death. We present an extensive structural and biochemical analysis of the yeast Pex1/6 complex. The heterohexamer forms a trimer of Pex1/6 dimers with a triangular geometry that is atypical for AAA+ complexes. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs. ATP hydrolysis results in a pumping motion of the complex, suggesting that Pex1/6 function involves substrate translocation through its central channel. Mutation of the Walker B motif in one D2 domain leads to ATP hydrolysis in the neighbouring domain, giving structural insights into inter-domain communication of these unique heterohexameric AAA+ assemblies.

Suggested Citation

  • Susanne Ciniawsky & Immanuel Grimm & Delia Saffian & Wolfgang Girzalsky & Ralf Erdmann & Petra Wendler, 2015. "Molecular snapshots of the Pex1/6 AAA+ complex in action," Nature Communications, Nature, vol. 6(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8331
    DOI: 10.1038/ncomms8331
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms8331
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms8331?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Maximilian Rüttermann & Michelle Koci & Pascal Lill & Ermis Dionysios Geladas & Farnusch Kaschani & Björn Udo Klink & Ralf Erdmann & Christos Gatsogiannis, 2023. "Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8331. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.