IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v401y1999i6754d10.1038_401717a0.html
   My bibliography  Save this article

Structural evidence for dimerization-regulated activation of an integral membrane phospholipase

Author

Listed:
  • H. J. Snijder

    (Laboratory of Biophysical Chemistry, BIOSON Research Institute, University of Groningen)

  • I. Ubarretxena-Belandia

    (Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University
    Yale University)

  • M. Blaauw

    (Laboratory of Biophysical Chemistry, BIOSON Research Institute, University of Groningen
    University of Groningen)

  • K. H. Kalk

    (Laboratory of Biophysical Chemistry, BIOSON Research Institute, University of Groningen)

  • H. M. Verheij

    (Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University)

  • M. R. Egmond

    (Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University)

  • N. Dekker

    (Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University)

  • B. W. Dijkstra

    (Laboratory of Biophysical Chemistry, BIOSON Research Institute, University of Groningen)

Abstract

Dimerization is a biological regulatory mechanism employed by both soluble and membrane proteins1. However, there are few structural data on the factors that govern dimerization of membrane proteins. Outer membrane phospholipase A (OMPLA) is an integral membrane enzyme which participates in secretion of colicins in Escherichia coli. In Campilobacter2 and Helicobacter pylori strains3, OMPLA is implied in virulence. Its activity is regulated by reversible dimerization4,5. Here we report X-ray structures of monomeric and dimeric OMPLA from E. coli. Dimer interactions occur almost exclusively in the apolar membrane-embedded parts, with two hydrogen bonds within the hydrophobic membrane area being key interactions. Dimerization results in functional oxyanion holes and substrate-binding pockets, which are absent in monomeric OMPLA. These results provide a detailed view of activation by dimerization of a membrane protein.

Suggested Citation

  • H. J. Snijder & I. Ubarretxena-Belandia & M. Blaauw & K. H. Kalk & H. M. Verheij & M. R. Egmond & N. Dekker & B. W. Dijkstra, 1999. "Structural evidence for dimerization-regulated activation of an integral membrane phospholipase," Nature, Nature, vol. 401(6754), pages 717-721, October.
    • Handle: RePEc:nat:nature:v:401:y:1999:i:6754:d:10.1038_401717a0
    DOI: 10.1038/401717a0
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/401717a0
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/401717a0?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. Irina V. Mikheyeva & Jiawei Sun & Kerwyn Casey Huang & Thomas J. Silhavy, 2023. "Mechanism of outer membrane destabilization by global reduction of protein content," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    2. Sarah E. Hanson & Tyrone Dowdy & Mioara Larion & Matthew Thomas Doyle & Harris D. Bernstein, 2024. "The patatin-like protein PlpD forms structurally dynamic homodimers in the Pseudomonas aeruginosa outer membrane," Nature Communications, Nature, vol. 15(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:401:y:1999:i:6754:d:10.1038_401717a0. 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.