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1ryt
From Proteopedia
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'''RUBRERYTHRIN''' | '''RUBRERYTHRIN''' | ||
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[[Category: Kurtz, D M.]] | [[Category: Kurtz, D M.]] | ||
[[Category: Nordlund, P.]] | [[Category: Nordlund, P.]] | ||
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| - | [[Category: | + | [[Category: Ferroxidase]] |
| - | [[Category: | + | [[Category: Iron]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:04:42 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:04, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 08:04:42 2008
