IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v457y2009i7233d10.1038_nature07611.html
   My bibliography  Save this article

Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonality

Author

Listed:
  • Kayo Nozawa

    (Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, B34 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan)

  • Patrick O’Donoghue

    (Department of Molecular Biophysics and Biochemistry,)

  • Sarath Gundllapalli

    (Department of Molecular Biophysics and Biochemistry,)

  • Yuhei Araiso

    (Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, B34 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan)

  • Ryuichiro Ishitani

    (Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan)

  • Takuya Umehara

    (Department of Molecular Biophysics and Biochemistry,)

  • Dieter Söll

    (Department of Molecular Biophysics and Biochemistry,
    Yale University, New Haven, Connecticut 06520-8114, USA)

  • Osamu Nureki

    (Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, B34 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan
    Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan)

Abstract

Pyrrolysine's route into proteins Pyrrolysine is known as the 22nd 'natural' amino acid, complementing the 20 standard or proteinogenic amino acids and selenocysteine. Although pyrrolysine appears rarely in proteins, the machinery to utilize it has existed since the time of the last universal common ancestor. It is inserted in proteins by a specific suppressor tRNA that recognizes the UAG stop codon. This pyrrolysine-specific tRNA, tRNAPyl, is charged by the tRNA synthetase PylRS. This work reports the determination of the structure of the orthogonal Desulfitobacterium hafniense tRNAPyl–PylRS pair, revealing the molecular basis of the orthogonality both in vivo and in vitro. The structure of the co-complex reveals the distinct interactions of the protein and tRNA that distinguish this pair from those which function with the 20 standard amino acids.

Suggested Citation

  • Kayo Nozawa & Patrick O’Donoghue & Sarath Gundllapalli & Yuhei Araiso & Ryuichiro Ishitani & Takuya Umehara & Dieter Söll & Osamu Nureki, 2009. "Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonality," Nature, Nature, vol. 457(7233), pages 1163-1167, February.
    • Handle: RePEc:nat:nature:v:457:y:2009:i:7233:d:10.1038_nature07611
    DOI: 10.1038/nature07611
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature07611
    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/nature07611?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:457:y:2009:i:7233:d:10.1038_nature07611. 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.