Structural and biochemical studies of serine acetyltransferase reveal why the parasite Entamoeba histolytica cannot form a cysteine synthase complex.

@article{Kumar2011StructuralAB,
  title={Structural and biochemical studies of serine acetyltransferase reveal why the parasite Entamoeba histolytica cannot form a cysteine synthase complex.},
  author={S Sudalai Kumar and I. Kaspar Raj and Isha Nagpal and Naidu Subbarao and Samudrala Gourinath},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 14},
  pages={12533-41}
}
Cysteine (Cys) plays a major role in growth and survival of the human parasite Entamoeba histolytica. We report here the crystal structure of serine acetyltransferase (SAT) isoform 1, a cysteine biosynthetic pathway enzyme from E. histolytica (EhSAT1) at 1.77 Å, in complex with its substrate serine (Ser) at 1.59 Å and inhibitor Cys at 1.78 Å resolution. EhSAT1 exists as a trimer both in solution as well as in crystal structure, unlike hexamers formed by other known SATs. The difference in… CONTINUE READING