Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus.

@article{Lauritsen2011StructureOT,
  title={Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus.},
  author={Iben Lauritsen and Martin Willemo{\"e}s and Kaj Jensen and Eva Johansson and Pernille Harris},
  journal={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2011},
  volume={67 Pt 2},
  pages={201-8}
}
CTP synthase catalyzes the last committed step in de novo pyrimidine-nucleotide biosynthesis. Active CTP synthase is a tetrameric enzyme composed of a dimer of dimers. The tetramer is favoured in the presence of the substrate nucleotides ATP and UTP; when saturated with nucleotide, the tetramer completely dominates the oligomeric state of the enzyme. Furthermore, phosphorylation has been shown to regulate the oligomeric states of the enzymes from yeast and human. The crystal structure of a… CONTINUE READING