IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v424y2003i6949d10.1038_nature01831.html
   My bibliography  Save this article

Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB

Author

Listed:
  • Sascha Gutmann

    (Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich))

  • Peter W. Haebel

    (Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich))

  • Laurent Metzinger

    (Biochimie Pharmaceutique UPRES JE2311, Université de Rennes I)

  • Markus Sutter

    (Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich))

  • Brice Felden

    (Biochimie Pharmaceutique UPRES JE2311, Université de Rennes I)

  • Nenad Ban

    (Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich))

Abstract

Accurate translation of genetic information into protein sequence depends on complete messenger RNA molecules. Truncated mRNAs cause synthesis of defective proteins, and arrest ribosomes at the end of their incomplete message. In bacteria, a hybrid RNA molecule that combines the functions of both transfer and messenger RNAs (called tmRNA) rescues stalled ribosomes, and targets aberrant, partially synthesized, proteins for proteolytic degradation1,2. Here we report the 3.2-Å-resolution structure of the tRNA-like domain of tmRNA (tmRNAΔ) in complex with small protein B (SmpB), a protein essential for biological functions of tmRNA. We find that the flexible RNA molecule adopts an open L-shaped conformation and SmpB binds to its elbow region, stabilizing the single-stranded D-loop in an extended conformation. The most striking feature of the structure of tmRNAΔ is a 90° rotation of the TΨC-arm around the helical axis. Owing to this unusual conformation, the SmpB–tmRNAΔ complex positioned into the A-site of the ribosome orients SmpB towards the small ribosomal subunit, and directs tmRNA towards the elongation-factor binding region of the ribosome. On the basis of this structure, we propose a model for the binding of tmRNA on the ribosome.

Suggested Citation

  • Sascha Gutmann & Peter W. Haebel & Laurent Metzinger & Markus Sutter & Brice Felden & Nenad Ban, 2003. "Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB," Nature, Nature, vol. 424(6949), pages 699-703, August.
  • Handle: RePEc:nat:nature:v:424:y:2003:i:6949:d:10.1038_nature01831
    DOI: 10.1038/nature01831
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature01831
    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/nature01831?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.

    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:424:y:2003:i:6949:d:10.1038_nature01831. 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.