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Article
Nature Structural Biology  3, 539 - 546 (1996)
doi:10.1038/nsb0696-539

The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains

Fredrick deMaré1, Donald M. Kurtz Jr2 & Pär Nordlund1

  1Department of Molecular Biology, Stockholm University, 106 91 Stockholm, Sweden

  2Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602, USA

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.

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