Crystal structure of (+)-delta-cadinene synthase from Gossypium arboreum and evolutionary divergence of metal binding motifs for catalysis.

@article{Gennadios2009CrystalSO,
  title={Crystal structure of (+)-delta-cadinene synthase from Gossypium arboreum and evolutionary divergence of metal binding motifs for catalysis.},
  author={Heather A Gennadios and Ver{\'o}nica Rebollar Gonz{\'a}lez and Luigi Di Costanzo and Amang Li and Fanglei Yu and David J. Miller and Rudolf K Allemann and David W Christianson},
  journal={Biochemistry},
  year={2009},
  volume={48 26},
  pages={6175-83}
}
(+)-Delta-cadinene synthase (DCS) from Gossypium arboreum (tree cotton) is a sesquiterpene cyclase that catalyzes the cyclization of farnesyl diphosphate in the first committed step of the biosynthesis of gossypol, a phytoalexin that defends the plant from bacterial and fungal pathogens. Here, we report the X-ray crystal structure of unliganded DCS at 2.4 A resolution and the structure of its complex with three putative Mg(2+) ions and the substrate analogue inhibitor 2-fluorofarnesyl… CONTINUE READING