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

H. J. Snijder, I. Ubarretxena-Belandia, M. Blaauw, K. H. Kalk, H. M. Verheij, M. R. Egmond, N. Dekker and B. W. Dijkstra
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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
M. Blaauw: Laboratory of Biophysical Chemistry, BIOSON Research Institute, 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

Nature, 1999, vol. 401, issue 6754, 717-721

Abstract: 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.

Date: 1999
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DOI: 10.1038/401717a0

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