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| | <StructureSection load='4wqc' size='340' side='right'caption='[[4wqc]], [[Resolution|resolution]] 1.56Å' scene=''> | | <StructureSection load='4wqc' size='340' side='right'caption='[[4wqc]], [[Resolution|resolution]] 1.56Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wqc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Allvd Allvd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WQC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Allochromatium_vinosum_DSM_180 Allochromatium vinosum DSM 180]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WQC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=THJ:THIOSULFATE'>THJ</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wq7|4wq7]]</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=4wqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wqc OCA], [https://pdbe.org/4wqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wqc RCSB], [https://www.ebi.ac.uk/pdbsum/4wqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wqc ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tsdA, Alvin_0091 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=572477 ALLVD])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiosulfate_dehydrogenase Thiosulfate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.2.2 1.8.2.2] </span></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=4wqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wqc OCA], [http://pdbe.org/4wqc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wqc RCSB], [http://www.ebi.ac.uk/pdbsum/4wqc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wqc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TSDA_ALLVD TSDA_ALLVD]] Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.<ref>PMID:16995898</ref> <ref>PMID:22779704</ref> | + | [https://www.uniprot.org/uniprot/TSDA_ALLVD TSDA_ALLVD] Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.<ref>PMID:16995898</ref> <ref>PMID:22779704</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Allvd]] | + | [[Category: Allochromatium vinosum DSM 180]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thiosulfate dehydrogenase]]
| + | [[Category: Archer M]] |
| - | [[Category: Archer, M]] | + | [[Category: Brito JA]] |
| - | [[Category: Brito, J A]] | + | [[Category: Dahl C]] |
| - | [[Category: Dahl, C]] | + | [[Category: Denkmann K]] |
| - | [[Category: Denkmann, K]] | + | [[Category: Pereira IAC]] |
| - | [[Category: Pereira, I A.C]] | + | |
| - | [[Category: C-type cytochrome]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Tetrathionate]]
| + | |
| - | [[Category: Tsda]]
| + | |
| Structural highlights
Function
TSDA_ALLVD Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.[1] [2]
Publication Abstract from PubMed
Although the oxidative condensation of two thiosulfate anions to tetrathionate constitutes a well-documented and significant part of the natural sulfur cycle little is known about the enzymes catalyzing this reaction. In the purple sulfur bacterium Allochromatium vinosum, the reaction is catalyzed by the periplasmic diheme c-type cytochrome thiosulfate dehydrogenase (TsdA). Here, we report the crystal structure of the 'as-isolated' form of A. vinosum TsdA to 1.98 A resolution, and those of several redox states of the enzyme to different resolutions. The protein contains two typical class I c-type cytochrome domains wrapped around two hemes axially coordinated by His-53/Cys-96 and His-164/Lys-208. These domains are very similar suggesting a gene duplication event during evolution. A ligand switch from Lys-208 to Met-209 is observed upon reduction of the enzyme. Cys-96 is an essential residue for catalysis with the specific activity of the enzyme being completely abolished in several TsdA-Cys-96 variants. TsdA-K208N, K208G and M209G variants were catalytically active in thiosulfate oxidation as well as in tetrathionate reduction, pointing to heme 2 as the electron exit point. In this study, we provide spectroscopic and structural evidence that the TsdA reaction cycle involves the transient presence of heme 1 in the high-spin state caused by movement of the Sgamma atom of Cys-96 out of the iron coordination sphere. Based on the presented data, we draw important conclusions about the enzyme and propose a possible reaction mechanism for TsdA.
Thiosulfate Dehydrogenase (TsdA) from Allochromatium vinosum: Structural and Functional Insights into Thiosulfate Oxidation.,Brito JA, Denkmann K, Pereira IA, Archer M, Dahl C J Biol Chem. 2015 Feb 11. pii: jbc.M114.623397. PMID:25673691[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hensen D, Sperling D, Truper HG, Brune DC, Dahl C. Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum. Mol Microbiol. 2006 Nov;62(3):794-810. Epub 2006 Sep 21. PMID:16995898 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05408.x
- ↑ Denkmann K, Grein F, Zigann R, Siemen A, Bergmann J, van Helmont S, Nicolai A, Pereira IA, Dahl C. Thiosulfate dehydrogenase: a widespread unusual acidophilic c-type cytochrome. Environ Microbiol. 2012 Oct;14(10):2673-88. doi:, 10.1111/j.1462-2920.2012.02820.x. Epub 2012 Jul 11. PMID:22779704 doi:http://dx.doi.org/10.1111/j.1462-2920.2012.02820.x
- ↑ Brito JA, Denkmann K, Pereira IA, Archer M, Dahl C. Thiosulfate Dehydrogenase (TsdA) from Allochromatium vinosum: Structural and Functional Insights into Thiosulfate Oxidation. J Biol Chem. 2015 Feb 11. pii: jbc.M114.623397. PMID:25673691 doi:http://dx.doi.org/10.1074/jbc.M114.623397
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