The B-type channel is a major route for iron entry into the ferroxidase center and central cavity of bacterioferritin.

Bacterioferritin is a bacterial iron storage and detoxification protein that is capable of forming a ferric oxyhydroxide mineral core within its central cavity. To do this, iron must traverse the bacterioferritin protein shell, which is expected to occur through one or more of the channels through the shell identified by structural studies. The size and negative electrostatic potential of the 24 B-type channels suggest that they could provide a route for iron into bacterioferritin.

Structure of a bacterial α2-macroglobulin reveals mimicry of eukaryotic innate immunity.

Alpha-2-macroglobulins (A2Ms) are plasma proteins that trap and inhibit a broad range of proteases and are major components of the eukaryotic innate immune system. Surprisingly, A2M-like proteins were identified in pathogenically invasive bacteria and species that colonize higher eukaryotes. Bacterial A2Ms are located in the periplasm where they are believed to provide protection to the cell by trapping external proteases through a covalent interaction with an activated thioester.

Fe-haem bound to Escherichia coli bacterioferritin accelerates iron core formation by an electron transfer mechanism.

BFR (bacterioferritin) is an iron storage and detoxification protein that differs from other ferritins by its ability to bind haem cofactors. Haem bound to BFR is believed to be involved in iron release and was previously thought not to play a role in iron core formation. Investigation of the effect of bound haem on formation of the iron core has been enabled in the present work by development of a method for reconstitution of BFR from Escherichia coli with exogenously added haem at elevated temperature in the presence of a relatively high concentration of sodium chloride.

Structural and mechanistic studies of a stabilized subunit dimer variant of Escherichia coli bacterioferritin identify residues required for core formation.

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.

Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor.

Alanine:glyoxylate aminotransferase-1 (AGT) is a human liver peroxisomal enzyme whose deficiency results in, primary hyperoxaluria type 1 (PH1), a fatal metabolic disease. AGT requires a pyridoxal phosphate (PLP) co-factor in its active site. The AGT gene usually exists in one of two polymorphic forms, the major and minor alleles.

Insights into SEN virus prevalence, transmission, and treatment in community-based persons and patients with liver disease referred to a liver disease unit.

To document the prevalence and routes of transmission of SEN virus (SEN-V) in community-based individuals and patients referred to a liver disease unit, stored serum samples obtained from 160 Canadian Inuit and 140 patients with liver disease were tested for SEN-V DNA by polymerase chain reaction. In the community-based population, SEN-V was present in 57 (36%) of 160 persons. SEN-V-positive individuals tended to be younger and were more often male.