Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 284, Issue 28, Pages 18873-18881Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M901747200
Keywords
-
Categories
Funding
- Canadian Institutes of Health Research/Canadian Blood Services
- Canadian Institutes of Health Research [MOP-49597, 83/B14704, BB/D001943/1]
- Biotechnology and Biological Sciences Research Council
- Canadian Foundation for Innovation to the University of British Columbia Laboratory of Molecular Biophysics
- Michael Smith Foundation for Health Sciences
- University of British Columbia Laboratory of Molecular Biophysics
- United States Department of Energy Office of Basic Energy Sciences and Office of Biological and Environmental Research
- National Institutes of Health
- National Center for Research Resources
- Biomedical Technology Program
- National Institute of General Medical Sciences
- BBSRC [BB/D001943/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D001943/1] Funding Source: researchfish
Ask authors/readers for more resources
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 angstrom 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available