2cb2 | pdb_00002cb2

Sulfur Oxygenase Reductase from Acidianus Ambivalens

spinqualitylabelsall models 2cb2, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cb2 is a 6 chain structure with sequence from Acidianus ambivalens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: CSS, FE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SOR_ACIAM Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA