IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v455y2008i7217d10.1038_nature07326.html
   My bibliography  Save this article

Structural insights into amino acid binding and gene control by a lysine riboswitch

Author

Listed:
  • Alexander Serganov

    (Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA)

  • Lili Huang

    (Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA)

  • Dinshaw J. Patel

    (Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA)

Abstract

Riboswitch mechanisms Riboswitches are structured RNAs that can bind a ligand such as a metabolite or nucleobase. Binding of the ligand affects the function of the RNA, so that they are often found in regulatory loops. In this work Patel and colleagues report the structure of a riboswitch that binds the amino acid lysine. The scaffold of the riboswitch is preassembled, but conformational changes occur upon binding lysine that direct further changes in the RNA downstream of the switch. Structures of the riboswitch with lysine analogues, including an antibiotic, provide some insight the development of resistance.

Suggested Citation

  • Alexander Serganov & Lili Huang & Dinshaw J. Patel, 2008. "Structural insights into amino acid binding and gene control by a lysine riboswitch," Nature, Nature, vol. 455(7217), pages 1263-1267, October.
  • Handle: RePEc:nat:nature:v:455:y:2008:i:7217:d:10.1038_nature07326
    DOI: 10.1038/nature07326
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature07326
    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/nature07326?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. Zhou Gong & Yunjie Zhao & Changjun Chen & Yong Duan & Yi Xiao, 2014. "Insights into Ligand Binding to PreQ1 Riboswitch Aptamer from Molecular Dynamics Simulations," PLOS ONE, Public Library of Science, vol. 9(3), pages 1-12, March.

    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:455:y:2008:i:7217:d:10.1038_nature07326. 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.