6G0I
Active Fe-PP1
Summary for 6G0I
| Entry DOI | 10.2210/pdb6g0i/pdb |
| Descriptor | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, PHOSPHATE ION, FE (III) ION, ... (5 entities in total) |
| Functional Keywords | phosphatase, iron, oxidative stress, cell cycle, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 37963.64 |
| Authors | Salvi, F.,Barabas, O.,Koehn, M. (deposition date: 2018-03-18, release date: 2018-11-21, Last modification date: 2024-10-09) |
| Primary citation | Salvi, F.,Trebacz, M.,Kokot, T.,Hoermann, B.,Rios, P.,Barabas, O.,Koehn, M. Effects of stably incorporated iron on protein phosphatase-1 structure and activity. FEBS Lett., 592:4028-4038, 2018 Cited by PubMed Abstract: Protein phosphatase-1 (PP1) drives a large amount of phosphoSer/Thr protein dephosphorylations in eukaryotes to counteract multiple kinases in signaling pathways. The phosphatase requires divalent metal cations for catalytic activity and contains iron naturally. Iron has been suggested to have an influence on PP1 activity through Fe and Fe oxidation states. However, much biochemical and all structural data have been obtained with recombinant PP1 containing Mn ions. Purifying iron-containing PP1 from Escherichia coli has thus far not been 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 electronic/redox properties of iron in PP1 activity and shed light on the difference in substrate specificity between iron- and manganese-containing PP1. PubMed: 30403291DOI: 10.1002/1873-3468.13284 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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