4YKH

Thirty minutes iron loaded human H ferritin

4YKH の概要

• エントリーDOI: 10.2210/pdb4ykh/pdb
• 関連するPDBエントリー: 4OYN 4Y08
• 分子名称: Ferritin heavy chain, BICINE, FE (II) ION, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, ferroxidase, ferritin heavy chain, iron homeostasis
• 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: 22332.40

構造登録者

Pozzi, C.,Di Pisa, F.,Mangani, S. (登録日: 2015-03-04, 公開日: 2015-09-09, 最終更新日: 2025-10-01)

主引用文献

Pozzi, C.,Di Pisa, F.,Bernacchioni, C.,Ciambellotti, S.,Turano, P.,Mangani, S.
Iron binding to human heavy-chain ferritin.
Acta Crystallogr.,Sect.D, 71:1909-1920, 2015

PubMed Abstract: Maxi-ferritins are ubiquitous iron-storage proteins with a common cage architecture made up of 24 identical subunits of five α-helices that drive iron biomineralization through catalytic iron(II) oxidation occurring at oxidoreductase sites (OS). Structures of iron-bound human H ferritin were solved at high resolution by freezing ferritin crystals at different time intervals after exposure to a ferrous salt. Multiple binding sites were identified that define the iron path from the entry ion channels to the oxidoreductase sites. Similar data are available for another vertebrate ferritin: the M protein from Rana catesbeiana. A comparative analysis of the iron sites in the two proteins identifies new reaction intermediates and underlines clear differences in the pattern of ligands that define the additional iron sites that precede the oxidoreductase binding sites along this path. Stopped-flow kinetics assays revealed that human H ferritin has different levels of activity compared with its R. catesbeiana counterpart. The role of the different pattern of transient iron-binding sites in the OS is discussed with respect to the observed differences in activity across the species.

PubMed: 26327381
DOI: 10.1107/S1399004715013073

実験手法

X-RAY DIFFRACTION (1.52 Å)