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

Daniel Martinez Molina, Anders Wetterholm, Andreas Kohl, Andrew A. McCarthy, Damian Niegowski, Eva Ohlson, Tove Hammarberg, Said Eshaghi (), Jesper Z. Haeggström () and Pär Nordlund ()
Additional contact information
Daniel Martinez Molina: Division of Biophysics,
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,
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,

Nature, 2007, vol. 448, issue 7153, 613-616

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.

Date: 2007
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DOI: 10.1038/nature06009

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