IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v495y2013i7440d10.1038_nature11899.html
   My bibliography  Save this article

Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state

Author

Listed:
  • Chikashi Toyoshima

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo)

  • Shiho Iwasawa

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo)

  • Haruo Ogawa

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo)

  • Ayami Hirata

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo)

  • Junko Tsueda

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo)

  • Giuseppe Inesi

    (California Pacific Medical Center Research Institute)

Abstract

The X-ray crystal structures of SERCA1a, a Ca2+-ATPase from the sarcoplasmic reticulum, in the presence and absence of sarcolipin are reported; the structures indicate that sarcolipin stabilizes SERCA1a in an ‘open’ state that has not been well characterised previously, in which SERCA1a has not yet accepted calcium into its two high-affinity binding sites.

Suggested Citation

  • Chikashi Toyoshima & Shiho Iwasawa & Haruo Ogawa & Ayami Hirata & Junko Tsueda & Giuseppe Inesi, 2013. "Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state," Nature, Nature, vol. 495(7440), pages 260-264, March.
    • Handle: RePEc:nat:nature:v:495:y:2013:i:7440:d:10.1038_nature11899
    DOI: 10.1038/nature11899
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature11899
    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/nature11899?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. Yingying Guo & Yuanyuan Zhang & Renhong Yan & Bangdong Huang & Fangfei Ye & Liushu Wu & Ximin Chi & Yi shi & Qiang Zhou, 2022. "Cryo-EM structures of recombinant human sodium-potassium pump determined in three different states," Nature Communications, Nature, vol. 13(1), pages 1-9, 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:495:y:2013:i:7440:d:10.1038_nature11899. 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.