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| | <StructureSection load='4pwa' size='340' side='right'caption='[[4pwa]], [[Resolution|resolution]] 2.19Å' scene=''> | | <StructureSection load='4pwa' size='340' side='right'caption='[[4pwa]], [[Resolution|resolution]] 2.19Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pwa]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ensifer_meliloti Ensifer meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PWA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pwa]] is a 4 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=4PWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PWA 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></td></tr> | + | </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></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pw9|4pw9]], [[4pw3|4pw3]]</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=4pwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pwa OCA], [https://pdbe.org/4pwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pwa RCSB], [https://www.ebi.ac.uk/pdbsum/4pwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pwa ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">R02831, SMc04048 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266834 Ensifer meliloti])</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=4pwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pwa OCA], [http://pdbe.org/4pwa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pwa RCSB], [http://www.ebi.ac.uk/pdbsum/4pwa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pwa ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q92M25_RHIME Q92M25_RHIME] |
| | <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: Ensifer meliloti]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Laming, E M]] | + | [[Category: Sinorhizobium meliloti 1021]] |
| - | [[Category: Maher, M J]] | + | [[Category: Laming EM]] |
| - | [[Category: McGrath, A P]] | + | [[Category: Maher MJ]] |
| - | [[Category: C-type cytochrome]] | + | [[Category: McGrath AP]] |
| - | [[Category: Electron transfer]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Heme]]
| + | |
| Structural highlights
Function
Q92M25_RHIME
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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