The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria.

@article{Metzger2009TheSO,
  title={The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria.},
  author={Ute Metzger and Christoph Schall and Georg E Zocher and Inge A Uns{\"o}ld and Edyta Stec and Shu-Ming Li and Lutz Heide and Thilo Stehle},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 34},
  pages={14309-14}
}
Ergot alkaloids are toxins and important pharmaceuticals that are produced biotechnologically on an industrial scale. The first committed step of ergot alkaloid biosynthesis is catalyzed by dimethylallyl tryptophan synthase (DMATS; EC 2.5.1.34). Orthologs of DMATS are found in many fungal genomes. We report here the x-ray structure of DMATS, determined at a resolution of 1.76 A. A complex of DMATS from Aspergillus fumigatus with its aromatic substrate L-tryptophan and with an analogue of its… CONTINUE READING