5LG2
Horse L type ferritin iron loaded for 60 minutes
Summary for 5LG2
| Entry DOI | 10.2210/pdb5lg2/pdb |
| Descriptor | Ferritin light chain, CADMIUM ION, FE (III) ION, ... (8 entities in total) |
| Functional Keywords | l-type, ferritin, mineralization, iron, metal binding protein |
| Biological source | Equus caballus (Horse) |
| Total number of polymer chains | 1 |
| Total formula weight | 20392.39 |
| Authors | Pozzi, C.,Di Pisa, F.,Mangani, S. (deposition date: 2016-07-05, release date: 2017-02-22, Last modification date: 2024-01-10) |
| Primary citation | Pozzi, C.,Ciambellotti, S.,Bernacchioni, C.,Di Pisa, F.,Mangani, S.,Turano, P. Chemistry at the protein-mineral interface in L-ferritin assists the assembly of a functional ( mu (3)-oxo)Tris[( mu (2)-peroxo)] triiron(III) cluster. Proc. Natl. Acad. Sci. U.S.A., 114:2580-2585, 2017 Cited by PubMed Abstract: X-ray structures of homopolymeric L-ferritin obtained by freezing protein crystals at increasing exposure times to a ferrous solution showed the progressive formation of a triiron cluster on the inner cage surface of each subunit. After 60 min exposure, a fully assembled (μ-oxo)Tris[(μ-peroxo)(μ-glutamato-κ:κ')](glutamato-κ)(diaquo)triiron(III) anionic cluster appears in human L-ferritin. Glu60, Glu61, and Glu64 provide the anchoring of the cluster to the protein cage. Glu57 shuttles incoming iron ions toward the cluster. We observed a similar metallocluster in horse spleen L-ferritin, indicating that it represents a common feature of mammalian L-ferritins. The structures suggest a mechanism for iron mineral formation at the protein interface. The functional significance of the observed patch of carboxylate side chains and resulting metallocluster for biomineralization emerges from the lower iron oxidation rate measured in the E60AE61AE64A variant of human L-ferritin, leading to the proposal that the observed metallocluster corresponds to the suggested, but yet unobserved, nucleation site of L-ferritin. PubMed: 28202724DOI: 10.1073/pnas.1614302114 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.22 Å) |
Structure validation
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