4ZJK

FIVE MINUTES IRON LOADED HUMAN H FERRITIN

Summary for 4ZJK

• Entry DOI: 10.2210/pdb4zjk/pdb
• Descriptor: Ferritin heavy chain, FE (II) ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, iron storage protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 22021.55

Authors

Pozzi, C.,Di Pisa, F.,Mangani, S. (deposition date: 2015-04-29, release date: 2015-09-09, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.56 Å)