The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity.

@article{Izard1999TheCS,
  title={The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity.},
  author={Tina Izard and Arie Geerlof},
  journal={The EMBO journal},
  year={1999},
  volume={18 8},
  pages={2021-30}
}
Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in bacteria that catalyses a rate-limiting step in coenzyme A (CoA) biosynthesis, by transferring an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA). Each phosphopantetheine adenylyltransferase (PPAT) subunit displays a dinucleotide-binding fold that is structurally similar to that in class I aminoacyl-tRNA synthetases. Superposition of bound adenylyl moieties from dPCoA in PPAT and ATP in… CONTINUE READING