2cb2
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
- | 2CB2 is a | + | 2CB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acidianus_ambivalens Acidianus ambivalens] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CB2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thermophilic]] | [[Category: thermophilic]] | ||
- | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:08:41 2007'' |
Revision as of 13:03, 5 November 2007
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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 FE as ligand. Structure known Active Site: AC1. 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 Mon Nov 5 15:08:41 2007
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