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| | <StructureSection load='2c9x' size='340' side='right'caption='[[2c9x]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2c9x' size='340' side='right'caption='[[2c9x]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2c9x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_8093 Atcc 8093]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C9X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2c9x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Starkeya_novella Starkeya novella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MSS:(MOLYBDOPTERIN-S,S)-OXO-MOLYBDENUM'>MSS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2blf|2blf]], [[2bpb|2bpb]], [[2ca3|2ca3]], [[2ca4|2ca4]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MSS:(MOLYBDOPTERIN-S,S)-OXO-MOLYBDENUM'>MSS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2c9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9x OCA], [http://pdbe.org/2c9x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c9x RCSB], [http://www.ebi.ac.uk/pdbsum/2c9x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9x 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=2c9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9x OCA], [https://pdbe.org/2c9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9x RCSB], [https://www.ebi.ac.uk/pdbsum/2c9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q9LA16_STANO Q9LA16_STANO]] The exact function is not known. Can catalyze the reduction of a variety of substrates like dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase.[SAAS:SAAS00086612] The exact function is not known. Can catalyze the reduction of a variety of substrates like dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase (By similarity). | + | [https://www.uniprot.org/uniprot/Q9LA16_ANCNO Q9LA16_ANCNO] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c9x_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c9x_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 8093]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bailey, S]] | + | [[Category: Starkeya novella]] |
| - | [[Category: Bernhardt, P]] | + | [[Category: Bailey S]] |
| - | [[Category: Enemark, J]] | + | [[Category: Bernhardt P]] |
| - | [[Category: Feng, C]] | + | [[Category: Enemark J]] |
| - | [[Category: Honeychurch, M J]] | + | [[Category: Feng C]] |
| - | [[Category: Kappler, U]] | + | [[Category: Honeychurch MJ]] |
| - | [[Category: Tollin, G]] | + | [[Category: Kappler U]] |
| - | [[Category: C-type cytochrome]]
| + | [[Category: Tollin G]] |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Molybdopterin]]
| + | |
| - | [[Category: Mutant]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Sulfite oxidase]]
| + | |
| Structural highlights
Function
Q9LA16_ANCNO
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
The sulfite dehydrogenase from Starkeya novella is the only known sulfite-oxidizing enzyme that forms a permanent heterodimeric complex between a molybdenum and a heme c-containing subunit and can be crystallized in an electron transfer competent conformation. Tyr236 is a highly conserved active site residue in sulfite oxidoreductases and has been shown to interact with a nearby arginine and a molybdenum-oxo ligand that is involved in catalysis. We have created a Tyr236 to Phe substitution in the SorAB sulfite dehydrogenase. The purified SDH(Y236F) protein has been characterized in terms of activity, structure, intramolecular electron transfer, and EPR properties. The substituted protein exhibited reduced turnover rates and substrate affinity as well as an altered reactivity toward molecular oxygen as an electron acceptor. Following reduction by sulfite and unlike SDH(WT), the substituted enzyme was reoxidized quickly in the presence of molecular oxygen, a process reminiscent of the reactions of the sulfite oxidases. SDH(Y236F) also exhibited the pH-dependent CW-EPR signals that are typically observed in vertebrate sulfite oxidases, allowing a direct link of CW-EPR properties to changes caused by a single-amino acid substitution. No quantifiable electron transfer was seen in laser flash photolysis experiments with SDH(Y236F). The crystal structure of SDH(Y236F) clearly shows that as a result of the substitution the hydrogen bonding network surrounding the active site is disturbed, resulting in an increased mobility of the nearby arginine. These disruptions underline the importance of Tyr236 for the integrity of the substrate binding site and the optimal alignment of Arg55, which appears to be necessary for efficient electron transfer.
Kinetic and structural evidence for the importance of Tyr236 for the integrity of the Mo active site in a bacterial sulfite dehydrogenase.,Kappler U, Bailey S, Feng C, Honeychurch MJ, Hanson GR, Bernhardt PV, Tollin G, Enemark JH Biochemistry. 2006 Aug 15;45(32):9696-705. PMID:16893171[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kappler U, Bailey S, Feng C, Honeychurch MJ, Hanson GR, Bernhardt PV, Tollin G, Enemark JH. Kinetic and structural evidence for the importance of Tyr236 for the integrity of the Mo active site in a bacterial sulfite dehydrogenase. Biochemistry. 2006 Aug 15;45(32):9696-705. PMID:16893171 doi:10.1021/bi060058b
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