IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v524y2015i7564d10.1038_nature14549.html
   My bibliography  Save this article

X-ray structure of a mammalian stearoyl-CoA desaturase

Author

Listed:
  • Yonghong Bai

    (Baylor College of Medicine)

  • Jason G. McCoy

    (Baylor College of Medicine)

  • Elena J. Levin

    (Baylor College of Medicine)

  • Pablo Sobrado

    (University of Wisconsin–Madison)

  • Kanagalaghatta R. Rajashankar

    (Cornell University, Argonne National Laboratory)

  • Brian G. Fox

    (University of Wisconsin–Madison)

  • Ming Zhou

    (Baylor College of Medicine)

Abstract

The crystal structure of mouse SCD1 bound to fatty acid stearoyl-CoA is solved at 2.6 Å resolution; the structure reveals a novel geometry for the dimetal centre, and the acyl chain of the bound fatty acid is shown to be shielded and shaped to a particular conformation by the enzyme, providing a structural basis for the selectivity of fatty acid metabolism.

Suggested Citation

  • Yonghong Bai & Jason G. McCoy & Elena J. Levin & Pablo Sobrado & Kanagalaghatta R. Rajashankar & Brian G. Fox & Ming Zhou, 2015. "X-ray structure of a mammalian stearoyl-CoA desaturase," Nature, Nature, vol. 524(7564), pages 252-256, August.
  • Handle: RePEc:nat:nature:v:524:y:2015:i:7564:d:10.1038_nature14549
    DOI: 10.1038/nature14549
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature14549
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature14549?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

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


    Cited by:

    1. Lie Wang & Ming Zhou, 2023. "Structure of a eukaryotic cholinephosphotransferase-1 reveals mechanisms of substrate recognition and catalysis," Nature Communications, Nature, vol. 14(1), pages 1-8, December.
    2. Xue Guo & Jianxiu Zhang & Lei Han & Juliet Lee & Shoshana C. Williams & Allison Forsberg & Yan Xu & Rachel Narehood Austin & Liang Feng, 2023. "Structure and mechanism of the alkane-oxidizing enzyme AlkB," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    3. Maria Thürmer & André Gollowitzer & Helmut Pein & Konstantin Neukirch & Elif Gelmez & Lorenz Waltl & Natalie Wielsch & René Winkler & Konstantin Löser & Julia Grander & Madlen Hotze & Sönke Harder & A, 2022. "PI(18:1/18:1) is a SCD1-derived lipokine that limits stress signaling," Nature Communications, Nature, vol. 13(1), pages 1-21, 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:nature:v:524:y:2015:i:7564:d:10.1038_nature14549. 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.