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

@article{Snijder1999StructuralEF,
  title={Structural evidence for dimerization-regulated activation of an integral membrane phospholipase},
  author={Harm J Snijder and Iban Ubarretxena-Belandia and Mieke Blaauw and Kor H. Kalk and Hubertus M. Verheij and Maarten R. Egmond and Niek Dekker and Bauke W Dijkstra},
  journal={Nature},
  year={1999},
  volume={401},
  pages={717-721}
}
Dimerization is a biological regulatory mechanism employed by both soluble and membrane proteins. 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 Campilobacter and Helicobacter pylori strains, OMPLA is implied in virulence. Its activity is regulated by reversible dimerization,. Here we report X-ray… CONTINUE READING

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