IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v385y1997i6614d10.1038_385365a0.html
   My bibliography  Save this article

Crystal structure of the NG domain from the signal-recognition particle receptor FtsY

Author

Listed:
  • Guillermo Montoya

    (Structural Biology Programme)

  • Cecilia Svensson

    (Structural Biology Programme)

  • Joen Luirink

    (Structural Biology Programme)

  • Irmgard Sinning

    (Structural Biology Programme)

Abstract

Newly synthesized proteins destined either for secretion or incorporation into membranes are targeted to the membrane translocation machinery by a ubiquitous system consisting of a signal-recognition particle (SRP) and its receptor1,2. Both the SRP receptor and the protein within the SRP that binds the signal sequence contain GTPases3,4. These two proteins, together with the RNA component of the SRP, form a complex5–7 and thereby regulate each other's GTPase activity8. Here we report the structure of the GTPase-containing portion of FtsY, the functional homologue of the SRP receptor of Escherichia coli9, at 2.2 Å resolution without bound nucleotide. This so-called NG domain displays similarities to the Ras-related GTPases, as well as features unique to the SRP-type GTPases10, such as a separate amino-terminal domain, an insertion within the p21ras (Ras) effector domain11, and a wide-open GTP-binding region. The structure explains the low affinity of FtsY for GTP, and suggests rearrangements that may occur on nucleotide binding. It also identifies regions potentially involved in the transmission of signals between domains and in interactions with regulatory proteins.

Suggested Citation

  • Guillermo Montoya & Cecilia Svensson & Joen Luirink & Irmgard Sinning, 1997. "Crystal structure of the NG domain from the signal-recognition particle receptor FtsY," Nature, Nature, vol. 385(6614), pages 365-368, January.
    • Handle: RePEc:nat:nature:v:385:y:1997:i:6614:d:10.1038_385365a0
    DOI: 10.1038/385365a0
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/385365a0
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/385365a0?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. Pascal F Egea & Hiro Tsuruta & Gladys P de Leon & Johanna Napetschnig & Peter Walter & Robert M Stroud, 2008. "Structures of the Signal Recognition Particle Receptor from the Archaeon Pyrococcus furiosus: Implications for the Targeting Step at the Membrane," PLOS ONE, Public Library of Science, vol. 3(11), pages 1-14, November.
    2. Laura Czech & Christopher-Nils Mais & Hanna Kratzat & Pinku Sarmah & Pietro Giammarinaro & Sven-Andreas Freibert & Hanna Folke Esser & Joanna Musial & Otto Berninghausen & Wieland Steinchen & Roland B, 2022. "Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp," Nature Communications, Nature, vol. 13(1), pages 1-14, 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:385:y:1997:i:6614:d:10.1038_385365a0. 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.