• Prosthetic group features
• Desulforedoxin in SWISS­PROT/TREMBL
• Desulforedoxin in alignment databases
• Desulforedoxin in 3­D databases
• References

Iron-sulphur cluster	Formal oxidation states
Fe(SCys)4	[Fe(Cys)4]1-; [Fe(Cys)4]2-

Desulforedoxin is a low molecular weight iron­containing bacterial protein possibly involved in electron transfer. It contains a single iron ion with distorted tetrahedral coordination geometry [1]. Desulfoferrodoxin is a fusion protein [2] containing N­terminal desulforedoxin­type domain [3].

The 3­D structure of desulforedoxin has been solved [1]. Desulforedoxin exists as a two­fold symmetric dimer. One monomer is composed of up­and­down four­stranded antiparallel ß­structure. This simple ß­structure is extended upon dimer formation, resulting in a small incomplete ß­barrel. The iron centre is located at the periphery of the molecule and is bound to four cysteinyl residues, with no other ligands in the close vicinity of the metal.

                            I  II
                        ,---C--C---.
                        |   \  /   |
                        |   [Fe]   |
                        |    |\    |
                        | ,--CC--. |
                        | |IV,III| |
                        | |      | |
                        | |    ,-' |
                  ¯OOC--|-'    |   |
                        |      `---'  
                      +H3N

Desulforedoxin in SWISS­PROT/TREMBL

DESR_DESGI

Desulforedoxin (dx); Desulfovibrio gigas

Desulforedoxin­type Fe(Cys)₄ proteins in alignment databases

Protein Superfamily	Protein Homology Domain	Pfam	LPFC 3­D alignment
00036; desulforedoxin 00212; desulfoferrodoxin	00116; desulforedoxin	-	-

PDB	scop	BSM	RELI Base	Header	¹
1dxg	1dxg	1dxg	1dxg	Desulforedoxin (oxidised) (dimer); Desulfovibrio gigas	MS6GK8

¹ Macromolecular Structures abstract. Full text is available to BioMedNet Members

References

1. Archer, M., Huber, R., Tavares, P., Moura, I., Moura, J.J.G., Carrondo, M.A., Sieker, L.C., LeGall, J. and Romão, M.J. (1995) Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 Å resolution: A novel non­heme iron protein structure. J. Mol. Biol. 251, 690-702.
2. Brumlik, M.J., Leroy, G., Bruschi, M. and Voordouw, G. (1990) The nucleotide sequence of the Desulfovibrio gigas desulforedoxin gene indicates that the Desulfovibrio vulgaris rbo gene originated from a gene fusion event. J. Bacteriol. 172, 7289-7292.
3. Moura, I., Tavares, P., Moura, J.J.G., Ravi, N., Huynh, B.­H., Liu, M.Y. and LeGall, J. (1990) Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center. J. Biol. Chem. 265, 21596-21602.

Bibliography on structural studies of desulforedoxin

Bibliography on structural studies of desulfoferrodoxin