ATP-induced structural change of dephosphocoenzyme A kinase from Thermus thermophilus HB8.

@article{Seto2005ATPinducedSC,
  title={ATP-induced structural change of dephosphocoenzyme A kinase from Thermus thermophilus HB8.},
  author={Azusa Seto and Kazutaka Murayama and Mitsutoshi Toyama and Akio Ebihara and Noriko Nakagawa and Seiki Kuramitsu and Mikako Shirouzu and Shigeyuki Yokoyama},
  journal={Proteins},
  year={2005},
  volume={58 1},
  pages={235-42}
}
Dephosphocoenzyme A kinase (DCK) catalyzes phosphorylation in the final step of coenzyme A (CoA) biosynthesis. In this phosphorylation process, domain movements play a very important role. To reveal the structural changes induced by ligand binding, we determined the crystal structure of DCK from Thermus thermophilus HB8 by the multiwavelength anomalous dispersion method at 2.8 A. The crystal structure includes three independent protein molecules in the asymmetric unit: One is a liganded form… CONTINUE READING