A conserved motif mediates both multimer formation and allosteric activation of phosphoglycerate mutase 5.

@article{Wilkins2014ACM,
  title={A conserved motif mediates both multimer formation and allosteric activation of phosphoglycerate mutase 5.},
  author={Jordan Maximillian Wilkins and Cyrus McConnell and Peter A. Tipton and Mark Hannink},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 36},
  pages={25137-48}
}
Phosphoglycerate mutase 5 (PGAM5) is an atypical mitochondrial Ser/Thr phosphatase that modulates mitochondrial dynamics and participates in both apoptotic and necrotic cell death. The mechanisms that regulate the phosphatase activity of PGAM5 are poorly understood. The C-terminal phosphoglycerate mutase domain of PGAM5 shares homology with the catalytic domains found in other members of the phosphoglycerate mutase family, including a conserved histidine that is absolutely required for… CONTINUE READING