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| | ==Wolinella succinogenes octaheme sulfite reductase MccA, form I== | | ==Wolinella succinogenes octaheme sulfite reductase MccA, form I== |
| - | <StructureSection load='4rkm' size='340' side='right' caption='[[4rkm]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4rkm' size='340' side='right'caption='[[4rkm]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rkm]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_succinogenes Vibrio succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RKM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RKM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rkm]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes_DSM_1740 Wolinella succinogenes DSM 1740]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RKM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO2:SULFUR+DIOXIDE'>SO2</scene>, <scene name='pdbligand=SX:SULFUR+OXIDE'>SX</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO2:SULFUR+DIOXIDE'>SO2</scene>, <scene name='pdbligand=SX:SULFUR+OXIDE'>SX</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rkn|4rkn]]</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=4rkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rkm OCA], [https://pdbe.org/4rkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rkm RCSB], [https://www.ebi.ac.uk/pdbsum/4rkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rkm ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mccA, WS0379 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273121 Vibrio succinogenes])</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=4rkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rkm OCA], [http://pdbe.org/4rkm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rkm RCSB], [http://www.ebi.ac.uk/pdbsum/4rkm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rkm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MCCA_WOLSU MCCA_WOLSU] Respiratory sulfite reductase that catalyzes the reduction of sulfite to sulfide in a single step, consuming six electrons in the process (PubMed:22040142, PubMed:25642962). Required for sulfite respiration under anaerobic growth conditions (PubMed:22040142). Has only marginal activity with nitrite.<ref>PMID:22040142</ref> <ref>PMID:25642962</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: Vibrio succinogenes]] | + | [[Category: Large Structures]] |
| - | [[Category: Einsle, O]] | + | [[Category: Wolinella succinogenes DSM 1740]] |
| - | [[Category: Hermann, B]] | + | [[Category: Einsle O]] |
| - | [[Category: Kern, M]] | + | [[Category: Hermann B]] |
| - | [[Category: Pietra, L La]] | + | [[Category: Kern M]] |
| - | [[Category: Simon, J]] | + | [[Category: La Pietra L]] |
| - | [[Category: Multiheme cytochrome c]]
| + | [[Category: Simon J]] |
| - | [[Category: Periplasmic]]
| + | |
| - | [[Category: Sulfite reductase]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
4rkm is a 12 chain structure with sequence from Wolinella succinogenes DSM 1740. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MCCA_WOLSU Respiratory sulfite reductase that catalyzes the reduction of sulfite to sulfide in a single step, consuming six electrons in the process (PubMed:22040142, PubMed:25642962). Required for sulfite respiration under anaerobic growth conditions (PubMed:22040142). Has only marginal activity with nitrite.[1] [2]
Publication Abstract from PubMed
The six-electron reduction of sulfite to sulfide is the pivot point of the biogeochemical cycle of the element sulfur. The octahaem cytochrome c MccA (also known as SirA) catalyses this reaction for dissimilatory sulfite utilization by various bacteria. It is distinct from known sulfite reductases because it has a substantially higher catalytic activity and a relatively low reactivity towards nitrite. The mechanistic reasons for the increased efficiency of MccA remain to be elucidated. Here we show that anoxically purified MccA exhibited a 2- to 5.5-fold higher specific sulfite reductase activity than the enzyme isolated under oxic conditions. We determined the three-dimensional structure of MccA to 2.2 A resolution by single-wavelength anomalous dispersion. We find a homotrimer with an unprecedented fold and haem arrangement, as well as a haem bound to a CX15CH motif. The heterobimetallic active-site haem 2 has a Cu(I) ion juxtaposed to a haem c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory haem-copper oxidases, the oxidation-labile Cu(I) centre of MccA did not seem to undergo a redox transition during catalysis. Intact MccA tightly bound SO2 at haem 2, a dehydration product of the substrate sulfite that was partially turned over due to photoreduction by X-ray irradiation, yielding the reaction intermediate SO. Our data show the biometal copper in a new context and function and provide a chemical rationale for the comparatively high catalytic activity of MccA.
The octahaem MccA is a haem c-copper sulfite reductase.,Hermann B, Kern M, La Pietra L, Simon J, Einsle O Nature. 2015 Feb 2. doi: 10.1038/nature14109. PMID:25642962[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kern M, Klotz MG, Simon J. The Wolinella succinogenes mcc gene cluster encodes an unconventional respiratory sulphite reduction system. Mol Microbiol. 2011 Dec;82(6):1515-30. PMID:22040142 doi:10.1111/j.1365-2958.2011.07906.x
- ↑ Hermann B, Kern M, La Pietra L, Simon J, Einsle O. The octahaem MccA is a haem c-copper sulfite reductase. Nature. 2015 Feb 2. doi: 10.1038/nature14109. PMID:25642962 doi:http://dx.doi.org/10.1038/nature14109
- ↑ Hermann B, Kern M, La Pietra L, Simon J, Einsle O. The octahaem MccA is a haem c-copper sulfite reductase. Nature. 2015 Feb 2. doi: 10.1038/nature14109. PMID:25642962 doi:http://dx.doi.org/10.1038/nature14109
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