IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-18401-z.html
   My bibliography  Save this article

Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex

Author

Listed:
  • B. O. Forsberg

    (Science for Life Laboratory, Stockholm University)

  • S. Aibara

    (Science for Life Laboratory, Stockholm University
    Max Planck Institute for Biophysical Chemistry)

  • R. J. Howard

    (Science for Life Laboratory, Stockholm University)

  • N. Mortezaei

    (Science for Life Laboratory, Stockholm University
    Vironova AB)

  • E. Lindahl

    (Science for Life Laboratory, Stockholm University
    Swedish eScience Research Center, KTH Royal Institute of Technology)

Abstract

The pyruvate dehydrogenase complex (PDC) is a multienzyme complex central to aerobic respiration, connecting glycolysis to mitochondrial oxidation of pyruvate. Similar to the E3-binding protein (E3BP) of mammalian PDC, PX selectively recruits E3 to the fungal PDC, but its divergent sequence suggests a distinct structural mechanism. Here, we report reconstructions of PDC from the filamentous fungus Neurospora crassa by cryo-electron microscopy, where we find protein X (PX) interior to the PDC core as opposed to substituting E2 core subunits as in mammals. Steric occlusion limits PX binding, resulting in predominantly tetrahedral symmetry, explaining previous observations in Saccharomyces cerevisiae. The PX-binding site is conserved in (and specific to) fungi, and complements possible C-terminal binding motifs in PX that are absent in mammalian E3BP. Consideration of multiple symmetries thus reveals a differential structural basis for E3BP-like function in fungal PDC.

Suggested Citation

  • B. O. Forsberg & S. Aibara & R. J. Howard & N. Mortezaei & E. Lindahl, 2020. "Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18401-z
    DOI: 10.1038/s41467-020-18401-z
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-18401-z
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-020-18401-z?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. Christian Tüting & Fotis L. Kyrilis & Johannes Müller & Marija Sorokina & Ioannis Skalidis & Farzad Hamdi & Yashar Sadian & Panagiotis L. Kastritis, 2021. "Cryo-EM snapshots of a native lysate provide structural insights into a metabolon-embedded transacetylase reaction," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    2. Lu Yang & Tristan Wagner & Ariel Mechaly & Alexandra Boyko & Eduardo M. Bruch & Daniela Megrian & Francesca Gubellini & Pedro M. Alzari & Marco Bellinzoni, 2023. "High resolution cryo-EM and crystallographic snapshots of the actinobacterial two-in-one 2-oxoglutarate dehydrogenase," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Björn O. Forsberg & Pranav N. M. Shah & Alister Burt, 2023. "A robust normalized local filter to estimate compositional heterogeneity directly from cryo-EM maps," Nature Communications, Nature, vol. 14(1), pages 1-11, 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:11:y:2020:i:1:d:10.1038_s41467-020-18401-z. 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.