Phosphoryl Transfer Reaction Snapshots in Crystals: INSIGHTS INTO THE MECHANISM OF PROTEIN KINASE A CATALYTIC SUBUNIT.

@article{Gerlits2015PhosphorylTR,
  title={Phosphoryl Transfer Reaction Snapshots in Crystals: INSIGHTS INTO THE MECHANISM OF PROTEIN KINASE A CATALYTIC SUBUNIT.},
  author={Oksana O. Gerlits and Jianhui Tian and Amit Das and Paul Langan and William T. Heller and Andrey Y Kovalevsky},
  journal={The Journal of biological chemistry},
  year={2015},
  volume={290 25},
  pages={15538-48}
}
To study the catalytic mechanism of phosphorylation catalyzed by cAMP-dependent protein kinase (PKA) a structure of the enzyme-substrate complex representing the Michaelis complex is of specific interest as it can shed light on the structure of the transition state. However, all previous crystal structures of the Michaelis complex mimics of the PKA catalytic subunit (PKAc) were obtained with either peptide inhibitors or ATP analogs. Here we utilized Ca(2+) ions and sulfur in place of the… CONTINUE READING