6tss | pdb_00006tss

Crystal structure of horse L ferritin (HoLf) Fe(III)-loaded for 60 minutes

spinqualitylabelsall models 6tss, resolution 2.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6tss 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. Ligands: CD, FE, O NonStd Res: CME Related: 6tsj, 6tsa, 6tsf, 6tr9, 6ts0, 6ts1, 6trz 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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