7O64
Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 1 minute.
Summary for 7O64
| Entry DOI | 10.2210/pdb7o64/pdb |
| Related | 7O63 |
| Descriptor | Ferritin, mitochondrial, FE (II) ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | human mitochondrial ferritin, hmtf, oxidoreductase, time-controlled iron loading, ferroxidase site |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 21279.02 |
| Authors | Pozzi, C.,Ciambellotti, S.,Tassone, G.,Turano, P.,Mangani, S. (deposition date: 2021-04-09, release date: 2021-10-13, Last modification date: 2024-01-31) |
| Primary citation | Ciambellotti, S.,Pratesi, A.,Tassone, G.,Turano, P.,Mangani, S.,Pozzi, C. Iron Binding in the Ferroxidase Site of Human Mitochondrial Ferritin. Chemistry, 27:14690-14701, 2021 Cited by PubMed Abstract: Ferritins are nanocage proteins that store iron ions in their central cavity as hydrated ferric oxide biominerals. In mammals, further the L (light) and H (heavy) chains constituting cytoplasmic maxi-ferritins, an additional type of ferritin has been identified, the mitochondrial ferritin (MTF). Human MTF (hMTF) is a functional homopolymeric H-like ferritin performing the ferroxidase activity in its ferroxidase site (FS), in which Fe(II) is oxidized to Fe(III) in the presence of dioxygen. To better investigate its ferroxidase properties, here we performed time-lapse X-ray crystallography analysis of hMTF, providing structural evidence of how iron ions interact with hMTF and of their binding to the FS. Transient iron binding sites, populating the pathway along the cage from the iron entry channel to the catalytic center, were also identified. Furthermore, our kinetic data at variable iron loads indicate that the catalytic iron oxidation reaction occurs via a diferric peroxo intermediate followed by the formation of ferric-oxo species, with significant differences with respect to human H-type ferritin. PubMed: 34343376DOI: 10.1002/chem.202102270 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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