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| | ==Crystal structure of the electron-transfer complex formed between a sulfite dehydrogenase and a c-type cytochrome from Sinorhizobium meliloti== | | ==Crystal structure of the electron-transfer complex formed between a sulfite dehydrogenase and a c-type cytochrome from Sinorhizobium meliloti== |
| - | <StructureSection load='4pw9' size='340' side='right' caption='[[4pw9]], [[Resolution|resolution]] 2.49Å' scene=''> | + | <StructureSection load='4pw9' size='340' side='right'caption='[[4pw9]], [[Resolution|resolution]] 2.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pw9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PW9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PW9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pw9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti_1021 Sinorhizobium meliloti 1021]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PW9 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></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]] 2.49Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pwa|4pwa]], [[4pw3|4pw3]]</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></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfite_oxidase Sulfite oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.1 1.8.3.1] </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=4pw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pw9 OCA], [https://pdbe.org/4pw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pw9 RCSB], [https://www.ebi.ac.uk/pdbsum/4pw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pw9 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=4pw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pw9 OCA], [http://pdbe.org/4pw9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pw9 RCSB], [http://www.ebi.ac.uk/pdbsum/4pw9 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q92M24_RHIME Q92M24_RHIME]] 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] | + | [https://www.uniprot.org/uniprot/Q92M24_RHIME Q92M24_RHIME] 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] |
| | <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: Sulfite oxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Maher, M J]] | + | [[Category: Sinorhizobium meliloti 1021]] |
| - | [[Category: McGrath, A P]] | + | [[Category: Maher MJ]] |
| - | [[Category: C-type cytochrome]] | + | [[Category: McGrath AP]] |
| - | [[Category: Electron transfer]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Electron-transfer complex]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Molybdopterin]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxidoreductase-electron transport complex]]
| + | |
| - | [[Category: Sulfite dehydrogenase]]
| + | |
| Structural highlights
Function
Q92M24_RHIME 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]
Publication Abstract from PubMed
Interprotein electron transfer underpins the essential processes of life and relies on the formation of specific, yet transient protein-protein interactions. In biological systems, the detoxification of sulfite is catalyzed by the sulfite-oxidizing enzymes (SOEs), which interact with an electron acceptor for catalytic turnover. Here, we report the structural and functional analyses of the SOE SorT from Sinorhizobium meliloti and its cognate electron acceptor SorU. Kinetic and thermodynamic analyses of the SorT/SorU interaction show the complex is dynamic in solution, and that the proteins interact with Kd = 13.5 +/- 0.8 muM. The crystal structures of the oxidized SorT and SorU, both in isolation and in complex, reveal the interface to be remarkably electrostatic, with an unusually large number of direct hydrogen bonding interactions. The assembly of the complex is accompanied by an adjustment in the structure of SorU, and conformational sampling provides a mechanism for dissociation of the SorT/SorU assembly.
Structural basis of interprotein electron transfer in bacterial sulfite oxidation.,McGrath AP, Laming EL, Casas Garcia GP, Kvansakul M, Guss JM, Trewhella J, Calmes B, Bernhardt PV, Hanson GR, Kappler U, Maher MJ Elife. 2015 Dec 19;4. pii: e09066. doi: 10.7554/eLife.09066. PMID:26687009[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McGrath AP, Laming EL, Casas Garcia GP, Kvansakul M, Guss JM, Trewhella J, Calmes B, Bernhardt PV, Hanson GR, Kappler U, Maher MJ. Structural basis of interprotein electron transfer in bacterial sulfite oxidation. Elife. 2015 Dec 19;4. pii: e09066. doi: 10.7554/eLife.09066. PMID:26687009 doi:http://dx.doi.org/10.7554/eLife.09066
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