1RYT

RUBRERYTHRIN

Summary for 1RYT

• Entry DOI: 10.2210/pdb1ryt/pdb
• Descriptor: RUBRERYTHRIN, FE (III) ION (3 entities in total)
• Functional Keywords: electron transport, iron, ferroxidase
• Biological source: Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
• Cellular location: Cytoplasm (Potential): P24931
• Total number of polymer chains: 1
• Total formula weight: 21613.62

Authors

Demare, F.,Kurtz, D.M.,Nordlund, P. (deposition date: 1996-04-26, release date: 1997-05-15, Last modification date: 2024-02-14)

Primary citation

deMare, F.,Kurtz Jr., D.M.,Nordlund, P.
The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains.
Nat.Struct.Biol., 3:539-546, 1996

PubMed Abstract: 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.

PubMed: 8646540
DOI: 10.1038/nsb0696-539

Experimental method

X-RAY DIFFRACTION (2.1 Å)