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| | <StructureSection load='2cb2' size='340' side='right'caption='[[2cb2]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='2cb2' size='340' side='right'caption='[[2cb2]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2cb2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciam Aciam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CB2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2cb2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidianus_ambivalens Acidianus ambivalens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CB2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cb2 OCA], [http://pdbe.org/2cb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2cb2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cb2 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cb2 OCA], [https://pdbe.org/2cb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cb2 RCSB], [https://www.ebi.ac.uk/pdbsum/2cb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cb2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SOR_ACIAM SOR_ACIAM] Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products.<ref>PMID:15030315</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aciam]] | + | [[Category: Acidianus ambivalens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Frazao, C]] | + | [[Category: Frazao C]] |
| - | [[Category: Gomes, C M]] | + | [[Category: Gomes CM]] |
| - | [[Category: Kletzin, A]] | + | [[Category: Kletzin A]] |
| - | [[Category: Urich, T]] | + | [[Category: Urich T]] |
| - | [[Category: 2-his-1- carboxylate facial triad]]
| + | |
| - | [[Category: Acidophilic]]
| + | |
| - | [[Category: Archaea]]
| + | |
| - | [[Category: Biogeochemical sulfur cycle]]
| + | |
| - | [[Category: Compartmentalization]]
| + | |
| - | [[Category: Cysteine persulphide]]
| + | |
| - | [[Category: Extremophile]]
| + | |
| - | [[Category: Icosatetramer]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Mononuclear non-heme iron]]
| + | |
| - | [[Category: Nano-structure]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Proto- organelle]]
| + | |
| - | [[Category: Sulfur oxygenase reductase]]
| + | |
| - | [[Category: Thermophilic]]
| + | |
| Structural highlights
Function
SOR_ACIAM Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Urich T, Bandeiras TM, Leal SS, Rachel R, Albrecht T, Zimmermann P, Scholz C, Teixeira M, Gomes CM, Kletzin A. The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre. Biochem J. 2004 Jul 1;381(Pt 1):137-46. PMID:15030315 doi:http://dx.doi.org/10.1042/BJ20040003
- ↑ Urich T, Gomes CM, Kletzin A, Frazao C. X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme. Science. 2006 Feb 17;311(5763):996-1000. PMID:16484493 doi:311/5763/996
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