Dataset for: Effects of stably incorporated iron on Protein Phosphatase-1 structure and activity

Protein phosphatase-1 (PP1) drives a large amount of phosphoSer/Thr protein dephosphorylations in eukaryotes, to counteract multiple kinases in signalling pathways. The phosphatase requires divalent metal cations for catalytic activity and contains naturally iron, which was suggested to have an influence on PP1 activity through Fe2+ and Fe3+ oxidation states. However, much biochemical and all structural data have been obtained with recombinant PP1 containing Mn2+ ions. Purifying iron-including PP1 from E. coli expression was so far not possible. Here, we present the preparation, characterization, and structure of iron-bound PP1α in inactive and active states. We establish a key role for the iron’s electronic/redox properties in PP1 activity, and shed light on the difference in substrate specificity between iron- and manganese-containing PP1.