2CB2
Sulfur Oxygenase Reductase from Acidianus Ambivalens
Summary for 2CB2
| Entry DOI | 10.2210/pdb2cb2/pdb |
| Descriptor | SULFUR OXYGENASE REDUCTASE, FE (III) ION (3 entities in total) |
| Functional Keywords | oxidoreductase, sulfur oxygenase reductase, mononuclear non-heme iron, biogeochemical sulfur cycle, extremophile, thermophilic, acidophilic, cysteine persulphide, icosatetramer, proto- organelle, nano-structure, compartmentalization, 2-his-1- carboxylate facial triad, archaea, metal-binding |
| Biological source | ACIDIANUS AMBIVALENS |
| Total number of polymer chains | 6 |
| Total formula weight | 218897.26 |
| Authors | Urich, T.,Gomes, C.M.,Kletzin, A.,Frazao, C. (deposition date: 2005-12-28, release date: 2006-02-24, Last modification date: 2024-11-13) |
| Primary citation | Urich, T.,Gomes, C.M.,Kletzin, A.,Frazao, C. X-Ray Structure of a Self-Compartmentalizing Sulfur Cycle Metalloenzyme Science, 311:996-, 2006 Cited by PubMed Abstract: Numerous microorganisms oxidize sulfur for energy conservation and contribute to the global biogeochemical sulfur cycle. We have determined the 1.7 angstrom-resolution structure of the sulfur oxygenase reductase from the thermoacidophilic archaeon Acidianus ambivalens, which catalyzes an oxygen-dependent disproportionation of elemental sulfur. Twenty-four monomers form a large hollow sphere enclosing a positively charged nanocompartment. Apolar channels provide access for linear sulfur species. A cysteine persulfide and a low-potential mononuclear non-heme iron site ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit constitute the active sites, accessible from the inside of the sphere. The iron is likely the site of both sulfur oxidation and sulfur reduction. PubMed: 16484493DOI: 10.1126/SCIENCE.1120306 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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