2cb2
From Proteopedia
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SULFUR OXYGENASE REDUCTASE FROM ACIDIANUS AMBIVALENS
Overview
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.
About this Structure
2CB2 is a Single protein structure of sequence from Acidianus ambivalens with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme., Urich T, Gomes CM, Kletzin A, Frazao C, Science. 2006 Feb 17;311(5763):996-1000. PMID:16484493
Page seeded by OCA on Sun Feb 3 10:33:33 2008
Categories: Acidianus ambivalens | Single protein | Frazao, C. | Gomes, C.M. | Kletzin, A. | Urich, T. | FE | 2-his-1-carboxylate facial triad | Acidophilic | Archaea | Biogeochemical sulfur cycle | Compartmentalization | Cysteine persulphide | Extremophile | Icosatetramer | Metal-binding | Mononuclear non-heme iron | Nano-structure | Oxidoreductase | Proto-organelle | Sulfur oxygenase reductase | Thermophilic
