7O6C

Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 15 minutes under anaerobic environment

7O6C の概要

• エントリーDOI: 10.2210/pdb7o6c/pdb
• 関連するPDBエントリー: 7O63 7O64 7O65 7O66 7O67 7O68 7O69
• 分子名称: Ferritin, mitochondrial, FE (II) ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: human mitochondrial ferritin, hmtf, time-controlled iron loading, ferroxidase site, oxidoreductase, anaerobic environment
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22090.14

構造登録者

Pozzi, C.,Ciambellotti, S.,Tassone, G.,Turano, P.,Mangani, S. (登録日: 2021-04-09, 公開日: 2021-10-13, 最終更新日: 2024-01-31)

主引用文献

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

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: 34343376
DOI: 10.1002/chem.202102270

実験手法

X-RAY DIFFRACTION (1.2 Å)