› 3e1n

X-ray diffraction
2.8Å resolution

Crystal structure of E. coli Bacterioferritin (BFR) after a 65 minute (aerobic) exposure to FE(II) revealing a possible MU-OXO bridge/MU-Hydroxy bridged DIIRON intermediate at the ferroxidase centre. (FE(III)-O-FE(III)-BFR).

Released:
DOI: 10.2210/pdb3e1n/pdb
PDB entry 3e1n coloured by chain, front view.
PDB entry 3e1n coloured by chain, side view.
PDB entry 3e1n coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural basis for iron mineralization by bacterioferritin.
Crow A, Lawson TL, Lewin A, Moore GR, Le Brun NE
J Am Chem Soc 131 6808-13 (2009)
PMID: 19391621

Function and Biology Details

Reaction catalysed: 
4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142039 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacterioferritin Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 158 amino acids
Theoretical weight: 18.52 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABD3 (Residues: 1-158; Coverage: 100%)
Gene names: JW3298, b3336, bfr
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

4 bound ligands:
Ligand SO4 16 x SO4
Ligand FE2 24 x FE2
Ligand UNK 12 x UNK
Ligand HEM 6 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P42212
Unit cell:
a: 207.741Å b: 207.741Å c: 142.951Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.25 0.268
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Ferritin: the protein nanocage and iron biomineral in health and in disease.
Theil EC. (2013)
7 more

2 mentions without citation

Iron Oxidation in Escherichia coli Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with H2 O2 but Slowly with O2.
Pullin et al. (2021)
1 more