5J8W
One minute iron loaded Rana Catesbeiana H' ferritin variant E57A/E136A/D140A
Summary for 5J8W
| Entry DOI | 10.2210/pdb5j8w/pdb |
| Related | 5J8S |
| Descriptor | Ferritin, middle subunit, FE (II) ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | rana catesbeiana, ferritin variant, ferroxidase activity, m type, h' type, oxidoreductase activity, iron, oxidoreductase |
| Biological source | Lithobates catesbeiana (American bullfrog) |
| Total number of polymer chains | 1 |
| Total formula weight | 21446.75 |
| Authors | Pozzi, C.,Di Pisa, F.,Mangani, S.,Bernacchioni, C.,Turano, P. (deposition date: 2016-04-08, release date: 2016-10-05, Last modification date: 2024-01-10) |
| Primary citation | Bernacchioni, C.,Pozzi, C.,Di Pisa, F.,Mangani, S.,Turano, P. Ferroxidase Activity in Eukaryotic Ferritin is Controlled by Accessory-Iron-Binding Sites in the Catalytic Cavity. Chemistry, 22:16213-16219, 2016 Cited by PubMed Abstract: Ferritins are iron-storage nanocage proteins that catalyze the oxidation of Fe to Fe at ferroxidase sites. By a combination of structural and spectroscopic techniques, Asp140, together with previously identified Glu57 and Glu136, is demonstrated to be an essential residue to promote the iron oxidation at the ferroxidase site. However, the presence of these three carboxylate moieties in close proximity to the catalytic centers is not essential to achieve binding of the Fe substrate to the diferric ferroxidase sites with the same coordination geometries as in the wild-type cages. PubMed: 27650996DOI: 10.1002/chem.201602842 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.11 Å) |
Structure validation
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