The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains.
We have determined the structure of rubrerythrin, a non-haem iron protein from the anaerobic sulphate-reducing bacterium, Desulfovibrio vulgaris (Hildenborough), by X-ray crystallography. The structure reveals a tetramer of two-domain subunits. Each subunit contains a four-helix bundle surrounding a diiron-oxo site and a C-terminal rubredoxin-like FeS4 domain. The diiron-oxo site contains a larger number of carboxylate ligands and a higher degree of solvent exposure than do those in other diiron-oxo proteins. The four-helix bundle of rubrerythrin closely resembles those of the ferritin and bacterioferritin subunits, suggesting a relationship among these proteins-consistent with the recently demonstrated ferroxidase activity of rubrerythrin.
deMaré
F
F
Department of Molecular Biology, Stockholm University, Sweden.
Kurtz
D M
DM
Nordlund
P
P
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D002570:Ceruloplasmin / Q000737:chemistry / Q000378:metabolism; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D003573:Cytochrome b Group / Q000737:chemistry / Q000378:metabolism; D016969:Desulfovibrio vulgaris / Q000737:chemistry*; D005288:Ferredoxins / Q000737:chemistry*; D005293:Ferritins / Q000737:chemistry / Q000378:metabolism; D006422:Hemerythrin; D007501:Iron / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012416:Rubredoxins / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D005288:Ferredoxins; D006422:Hemerythrin; D012416:Rubredoxins; C055857:rubrerythrins; D005293:Ferritins; C018032:bacterioferritin; D007501:Iron; D002570:Ceruloplasmin