Structural highlights
6tsx is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 2.021Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
FRIL_HORSE Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
Publication Abstract from PubMed
X-ray structures of homopolymeric human L-ferritin and horse spleen ferritin were solved by freezing protein crystals at different time intervals after exposure to a ferric salt and revealed the growth of an octa-nuclear iron cluster on the inner surface of the protein cage with a key role played by some glutamate residues. An atomic resolution view of how the cluster formation develops starting from a (mu 3 -oxo)tris[(mu 2 -glutamato-kappaO:kappaO')](glutamato-kappaO)(diaquo)triiron(III) seed is provided. The results support the idea that iron biomineralization in ferritin is a process initiating at the level of the protein surface, capable of contributing coordination bonds and electrostatic guidance.
Iron biomineral growth from the initial nucleation seed in L-ferritin.,Ciambellotti S, Pozzi C, Mangani S, Turano P Chemistry. 2020 Feb 6. doi: 10.1002/chem.202000064. PMID:32027764[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ciambellotti S, Pozzi C, Mangani S, Turano P. Iron biomineral growth from the initial nucleation seed in L-ferritin. Chemistry. 2020 Feb 6. doi: 10.1002/chem.202000064. PMID:32027764 doi:http://dx.doi.org/10.1002/chem.202000064
