6TS1

Crystal structure of human L ferritin (HuLf) triple variant E60A-E61A-E64A Fe(III)-loaded for 60 minutes

This is a non-PDB format compatible entry.

Summary for 6TS1

• Entry DOI: 10.2210/pdb6ts1/pdb
• Related: 6TR9 6TRZ 6TS0
• Descriptor: Ferritin light chain, OXYGEN ATOM, CADMIUM ION, ... (6 entities in total)
• Functional Keywords: human l ferritin, hulf, e60a-e61a-e64a, fe(iii), trinuclear fe(iii) cluster, metal binding protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 20597.68

Authors

Pozzi, C.,Ciambellotti, S.,Turano, P.,Mangani, S. (deposition date: 2019-12-19, release date: 2020-02-19, Last modification date: 2024-01-24)

Primary citation

Ciambellotti, S.,Pozzi, C.,Mangani, S.,Turano, P.
Iron Biomineral Growth from the Initial Nucleation Seed in L-Ferritin.
Chemistry, 26:5770-5773, 2020

PubMed Abstract: 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 (μ -oxo)tris[(μ -glutamato-κO:κO')](glutamato-κO)(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.

PubMed: 32027764
DOI: 10.1002/chem.202000064

Experimental method

X-RAY DIFFRACTION (2.2 Å)