Energetics of outer membrane phospholipase A (OMPLA) dimerization.

@article{Stanley2006EnergeticsOO,
  title={Energetics of outer membrane phospholipase A (OMPLA) dimerization.},
  author={Ann Marie Stanley and Pitak Chuawong and Tamara L. Hendrickson and Karen G Fleming},
  journal={Journal of molecular biology},
  year={2006},
  volume={358 1},
  pages={
          120-31
        }
}
Outer membrane phospholipase A (OMPLA) is a widely conserved transmembrane enzyme found in Gram-negative bacteria, and it is implicated in the virulence of a number of pathogenic organisms. The regulation of the protein's phospholipase activity is not well understood despite the existence of a number of high resolution structures. Previous biochemical studies have demonstrated that dimerization of OMPLA is a prerequisite for its phospholipase activity, and it has been shown in vitro that this… CONTINUE READING
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