1ryt
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(New page: 200px<br /><applet load="1ryt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ryt, resolution 2.1Å" /> '''RUBRERYTHRIN'''<br />...)
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Revision as of 23:51, 20 November 2007
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RUBRERYTHRIN
Overview
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.
About this Structure
1RYT is a Single protein structure of sequence from Desulfovibrio vulgaris with FE as ligand. Full crystallographic information is available from OCA.
Reference
The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains., deMare F, Kurtz DM Jr, Nordlund P, Nat Struct Biol. 1996 Jun;3(6):539-46. PMID:8646540
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