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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
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    Cited by:

    1. 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.
    2. 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.

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