InterPro domain: IPR024935

Rubredoxin is a low molecular weight iron-containing bacterial protein involved in electron transfer [ 1 , 2 ], sometimes replacing ferredoxin as an electron carrier [ 3 ]. Rubredoxins possess a 45- to 55-residue domain containing one iron atom tetrahedrally coordinated to four cysteinyl residues. Structural analysis of the domains have shown them to be folded into a short three-stranded antiparallel beta-sheet and a number of loops [ 4 , 5 , 6 , 7 ].

This entry represents the rubredoxin domain.

1. Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data. Biochem. J. 271, 839-41
2. Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 A resolution. J. Mol. Biol. 217, 337-52
3. Isolation, characterization, and primary structure of rubredoxin from the photosynthetic bacterium, Heliobacillus mobilis. Arch. Biochem. Biophys. 318, 80-8
4. Rubredoxin from Desulfovibrio gigas. A molecular model of the oxidized form at 1.4 A resolution. J. Mol. Biol. 197, 525-41
5. X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus. Protein Sci. 1, 1494-507
6. Rubredoxin in crystalline state. Meth. Enzymol. 243, 203-16
7. The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains. Nat. Struct. Biol. 3, 539-46