Structural highlights
3e2c is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , |
| Gene: | bfr, b3336, JW3298 (ECOLI) |
| Activity: | Ferroxidase, with EC number 1.16.3.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[BFR_ECOLI] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bacterioferritin (BFR) is a bacterial member of the ferritin family that functions in iron metabolism and protects against oxidative stress. BFR differs from the mammalian protein in that it is comprised of 24 identical subunits and is able to bind 12 equivalents of heme at sites located between adjacent pairs of subunits. The mechanism by which iron enters the protein to form the dinuclear (ferroxidase) catalytic site present in every subunit and the mineralized iron core housed within the 24-mer is not well understood. To address this issue, the properties of a catalytically functional assembly variant (E128R/E135R) of Escherichia coli BFR are characterized by a combination of crystallography, site-directed mutagenesis, and kinetics. The three-dimensional structure of the protein (1.8 A resolution) includes two ethylene glycol molecules located on either side of the dinuclear iron site. One of these ethylene glycol molecules is integrated into the surface of the protein that would normally be exposed to solvent, and the other is integrated into the surface of the protein that would normally face the iron core where it is surrounded by the anionic residues Glu(47), Asp(50), and Asp(126). We propose that the sites occupied by these ethylene glycol molecules define regions where iron interacts with the protein, and, in keeping with this proposal, ferroxidase activity decreases significantly when they are replaced with the corresponding amides.
Structural and Mechanistic Studies of a Stabilized Subunit Dimer Variant of Escherichia coli Bacterioferritin Identify Residues Required for Core Formation.,Wong SG, Tom-Yew SA, Lewin A, Le Brun NE, Moore GR, Murphy ME, Mauk AG J Biol Chem. 2009 Jul 10;284(28):18873-81. Epub 2009 May 13. PMID:19439409[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yang X, Le Brun NE, Thomson AJ, Moore GR, Chasteen ND. The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Biochemistry. 2000 Apr 25;39(16):4915-23. PMID:10769150
- ↑ Baaghil S, Lewin A, Moore GR, Le Brun NE. Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center. Biochemistry. 2003 Dec 2;42(47):14047-56. PMID:14636073 doi:http://dx.doi.org/10.1021/bi035253u
- ↑ Wong SG, Tom-Yew SA, Lewin A, Le Brun NE, Moore GR, Murphy ME, Mauk AG. Structural and Mechanistic Studies of a Stabilized Subunit Dimer Variant of Escherichia coli Bacterioferritin Identify Residues Required for Core Formation. J Biol Chem. 2009 Jul 10;284(28):18873-81. Epub 2009 May 13. PMID:19439409 doi:M901747200
