IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v521y2015i7553d10.1038_nature14247.html
   My bibliography  Save this article

Atomic structure of anthrax protective antigen pore elucidates toxin translocation

Author

Listed:
  • Jiansen Jiang

    (Immunology and Molecular Genetics, University of California
    California NanoSystems Institute, University of California)

  • Bradley L. Pentelute

    (Massachusetts Institute of Technology)

  • R. John Collier

    (Harvard Medical School)

  • Z. Hong Zhou

    (Immunology and Molecular Genetics, University of California
    California NanoSystems Institute, University of California)

Abstract

Cryo-electron microscopy determination of anthrax toxin protective antigen pore structure at a resolution of 2.9 Å, revealing the catalytic Φ-clamp and the membrane-spanning translocation channel.

Suggested Citation

  • Jiansen Jiang & Bradley L. Pentelute & R. John Collier & Z. Hong Zhou, 2015. "Atomic structure of anthrax protective antigen pore elucidates toxin translocation," Nature, Nature, vol. 521(7553), pages 545-549, May.
    • Handle: RePEc:nat:nature:v:521:y:2015:i:7553:d:10.1038_nature14247
    DOI: 10.1038/nature14247
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature14247
    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/nature14247?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. Johnny Lisboa & Cassilda Pereira & Rute D. Pinto & Inês S. Rodrigues & Liliana M. G. Pereira & Bruno Pinheiro & Pedro Oliveira & Pedro José Barbosa Pereira & Jorge E. Azevedo & Dominique Durand & Rola, 2023. "Unconventional structure and mechanisms for membrane interaction and translocation of the NF-κB-targeting toxin AIP56," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Akihiro Kawamoto & Tomohito Yamada & Toru Yoshida & Yusui Sato & Takayuki Kato & Hideaki Tsuge, 2022. "Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile," Nature Communications, Nature, vol. 13(1), pages 1-12, 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:521:y:2015:i:7553:d:10.1038_nature14247. 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.