4pwa
From Proteopedia
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==Crystal structure of the c-type cytochrome SorU from Sinorhizobium meliloti== | ==Crystal structure of the c-type cytochrome SorU from Sinorhizobium meliloti== | ||
<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=''> | ||
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</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"><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='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'>[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://www.rcsb.org/pdb/explore.do?structureId=4pwa RCSB], [http://www.ebi.ac.uk/pdbsum/4pwa PDBsum]</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=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]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:26687009</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4pwa" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 19:02, 20 February 2016
Crystal structure of the c-type cytochrome SorU from Sinorhizobium meliloti
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