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Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase

Author

Listed:
  • Daniel Martinez Molina

    (Division of Biophysics,
    Stockholm University, S-106 91 Stockholm, Sweden)

  • Anders Wetterholm

    (Division of Chemistry 2, Department of Medical Biochemistry and Biophysics)

  • Andreas Kohl

    (Division of Biophysics,)

  • Andrew A. McCarthy

    (European Molecular Biology Laboratory, Grenoble outstation, 6 Rue Jules Horowitz, 38042 Grenoble Cedex 9, France)

  • Damian Niegowski

    (Division of Biophysics,
    Stockholm University, S-106 91 Stockholm, Sweden)

  • Eva Ohlson

    (Division of Chemistry 2, Department of Medical Biochemistry and Biophysics)

  • Tove Hammarberg

    (Division of Chemistry 2, Department of Medical Biochemistry and Biophysics)

  • Said Eshaghi

    (Division of Biophysics,)

  • Jesper Z. Haeggström

    (Division of Chemistry 2, Department of Medical Biochemistry and Biophysics)

  • Pär Nordlund

    (Division of Biophysics,
    Structural Genomics Consortium, Karolinska Institutet, 17177 Stockholm, Sweden)

Abstract

The X-ray crystal structure of human leukotriene C4 synthase, in its apo- and glutathione -complexed forms at 2.00 and 2.15 Å resolution, respectively, is solved. The structure of the enzyme in complex with substrate reveals that the active site enforces a horseshoe-shaped conformation of glutathione and positions its thiol group in a way that explains the selectivity of its chemical reaction.

Suggested Citation

  • Daniel Martinez Molina & Anders Wetterholm & Andreas Kohl & Andrew A. McCarthy & Damian Niegowski & Eva Ohlson & Tove Hammarberg & Said Eshaghi & Jesper Z. Haeggström & Pär Nordlund, 2007. "Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase," Nature, Nature, vol. 448(7153), pages 613-616, August.
    • Handle: RePEc:nat:nature:v:448:y:2007:i:7153:d:10.1038_nature06009
    DOI: 10.1038/nature06009
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