IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v391y1998i6668d10.1038_35563.html
   My bibliography  Save this article

Crystal structure of the yeast MATα2/MCM1/DNA ternary complex

Author

Listed:
  • Song Tan

    (ETH-Zürich, Institut för Molekularbiologie und Biophysik)

  • Timothy J. Richmond

    (ETH-Zürich, Institut för Molekularbiologie und Biophysik)

Abstract

The structure of a complex containing the homeodomain repressor protein MATα2 and the MADS-box transcription factor MCM1 bound to DNA has been determined by X-ray crystallography at 2.25 Å resolution. It reveals the protein–protein interactions responsible for cooperative binding of MATα2 and MCM1 to DNA. The otherwise flexible amino-terminal extension of the MATα2 homeodomain forms a β-hairpin that grips the MCM1 surface through parallel β-strand hydrogen bonds and close-packed, predominantly hydrophobic, side chains. DNA bending induced by MCM1 brings the two proteins closer together, facilitating their interaction. An unusual feature of the complex is that an eight-amino-acid sequence adopts an α-helical conformation in one of two copies of the MATα2 monomer and a β-strand conformation in the other. This ‘chameleon’ sequence of MATα2 may be important for recognizing natural operator sites.

Suggested Citation

  • Song Tan & Timothy J. Richmond, 1998. "Crystal structure of the yeast MATα2/MCM1/DNA ternary complex," Nature, Nature, vol. 391(6668), pages 660-666, February.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6668:d:10.1038_35563
    DOI: 10.1038/35563
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/35563
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/35563?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:391:y:1998:i:6668:d:10.1038_35563. 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.