1ryt
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ryt |SIZE=350|CAPTION= <scene name='initialview01'>1ryt</scene>, resolution 2.1Å | |PDB= 1ryt |SIZE=350|CAPTION= <scene name='initialview01'>1ryt</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene> | + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ryt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ryt OCA], [http://www.ebi.ac.uk/pdbsum/1ryt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ryt RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Kurtz, D M.]] | [[Category: Kurtz, D M.]] | ||
[[Category: Nordlund, P.]] | [[Category: Nordlund, P.]] | ||
| - | [[Category: FE]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: ferroxidase]] | [[Category: ferroxidase]] | ||
[[Category: iron]] | [[Category: iron]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:34:54 2008'' |
Revision as of 20:34, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 23:34:54 2008
