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NMR structures of phospholipase A2 reveal conformational changes during interfacial activation

Nature Structural Biology volume 2, pages 402–406 (1995)Cite this article

Abstract

It has long been proposed that the higher activity of phospholipase A2 (PLA2) for substrates presented as multimolecular aggregates compared to dispersed molecules (interfacial activation) arises due to a conformational change in the enzyme. X-ray studies have, however, failed to identify any such change. Here we report the solution structures of porcine pancreatic PLA2 both free and as a ternary complex with micelles and a competitive inhibitor. Important differences between these structures indicate that conformational changes may play an important role in the mechanism of interfacial activation in PLA2s.

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Authors and Affiliations

  1. Department of Enzymology and Protein Engineering, Utrecht University, Centre for Biomembranes and Lipid Enzymology, Padualaan 8, 3584 CH, Utrecht, The Netherlands

    Bert van den Berg, Ruud Dijkman, Gerard H. de Hass & Hubertus M. Verheij

  2. Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands

    Marco Tessari, Rolf Boelens & Robert Kaptein

Authors
  1. Bert van den Berg
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  2. Marco Tessari
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  7. Hubertus M. Verheij
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den Berg, B., Tessari, M., Boelens, R. et al. NMR structures of phospholipase A2 reveal conformational changes during interfacial activation. Nat Struct Mol Biol 2, 402–406 (1995). https://doi.org/10.1038/nsb0595-402

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