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| | ==Structure of the dissimilatory sulfite reductase from Archaeoglobus fulgidus== | | ==Structure of the dissimilatory sulfite reductase from Archaeoglobus fulgidus== |
| - | <StructureSection load='3mmc' size='340' side='right' caption='[[3mmc]], [[Resolution|resolution]] 2.04Å' scene=''> | + | <StructureSection load='3mmc' size='340' side='right'caption='[[3mmc]], [[Resolution|resolution]] 2.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3mmc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3c7b 3c7b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MMC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3mmc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3c7b 3c7b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MMC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</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]] 2.04Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c7b|3c7b]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogensulfite_reductase Hydrogensulfite reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.99.3 1.8.99.3] </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=3mmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mmc OCA], [https://pdbe.org/3mmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mmc RCSB], [https://www.ebi.ac.uk/pdbsum/3mmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mmc ProSAT]</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=3mmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mmc OCA], [http://pdbe.org/3mmc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mmc RCSB], [http://www.ebi.ac.uk/pdbsum/3mmc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mmc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DSRA_ARCFU DSRA_ARCFU]] Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration. [[http://www.uniprot.org/uniprot/DSRB_ARCFU DSRB_ARCFU]] Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration. | + | [https://www.uniprot.org/uniprot/DSRA_ARCFU DSRA_ARCFU] Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/3mmc_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/3mmc_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Archaeoglobus fulgidus]] | | [[Category: Archaeoglobus fulgidus]] |
| - | [[Category: Hydrogensulfite reductase]] | + | [[Category: Large Structures]] |
| - | [[Category: Diederichs, K]] | + | [[Category: Diederichs K]] |
| - | [[Category: Ermler, U]] | + | [[Category: Ermler U]] |
| - | [[Category: Huber, H]] | + | [[Category: Huber H]] |
| - | [[Category: Kroneck, P M.H]] | + | [[Category: Kroneck PMH]] |
| - | [[Category: Parey, K]] | + | [[Category: Parey K]] |
| - | [[Category: Schiffer, A]] | + | [[Category: Schiffer A]] |
| - | [[Category: Stetter, K O]] | + | [[Category: Stetter KO]] |
| - | [[Category: Warkentin, E]] | + | [[Category: Warkentin E]] |
| - | [[Category: Alpha-beta-protein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
DSRA_ARCFU Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration.
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
Conservation of energy based on the reduction of sulfate is of fundamental importance for the biogeochemical sulfur cycle. A key enzyme of this ancient anaerobic process is the dissimilatory sulfite reductase (dSir), which catalyzes the six-electron reduction of sulfite to hydrogen sulfide under participation of a unique magnetically coupled siroheme-[4Fe-4S] center. We determined the crystal structure of the enzyme from the sulfate-reducing archaeon Archaeoglobus fulgidus at 2-A resolution and compared it with that of the phylogenetically related assimilatory Sir (aSir). dSir is organized as a heterotetrameric (alphabeta)(2) complex composed of two catalytically independent alphabeta heterodimers. In contrast, aSir is a monomeric protein built of two fused modules that are structurally related to subunits alpha and beta except for a ferredoxin domain inserted only into the subunits of dSir. The [4Fe-4S] cluster of this ferredoxin domain is considered as the terminal redox site of the electron transfer pathway to the siroheme-[4Fe-4S] center in dSir. While aSir binds one siroheme-[4Fe-4S] center, dSir harbors two of them within each alphabeta heterodimer. Surprisingly, only one siroheme-[4Fe-4S] center in each alphabeta heterodimer is catalytically active, whereas access to the second one is blocked by a tryptophan residue. The spatial proximity of the functional and structural siroheme-[4Fe-4S] centers suggests that the catalytic activity at one active site was optimized during evolution at the expense of the enzymatic competence of the other. The sulfite binding mode and presumably the mechanism of sulfite reduction appear to be largely conserved between dSir and aSir. In addition, a scenario for the evolution of Sirs is proposed.
Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus.,Schiffer A, Parey K, Warkentin E, Diederichs K, Huber H, Stetter KO, Kroneck PM, Ermler U J Mol Biol. 2008 Jun 20;379(5):1063-74. Epub 2008 May 20. PMID:18495156[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schiffer A, Parey K, Warkentin E, Diederichs K, Huber H, Stetter KO, Kroneck PM, Ermler U. Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus. J Mol Biol. 2008 Jun 20;379(5):1063-74. Epub 2008 May 20. PMID:18495156 doi:10.1016/j.jmb.2008.04.027
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