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| | <StructureSection load='6o8n' size='340' side='right'caption='[[6o8n]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='6o8n' size='340' side='right'caption='[[6o8n]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6o8n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O8N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6O8N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6o8n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O8N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 1.95Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</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://proteopedia.org/fgij/fg.htm?mol=6o8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o8n OCA], [http://pdbe.org/6o8n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o8n RCSB], [http://www.ebi.ac.uk/pdbsum/6o8n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o8n 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=6o8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o8n OCA], [https://pdbe.org/6o8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o8n RCSB], [https://www.ebi.ac.uk/pdbsum/6o8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o8n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D5AT91_RHOCB D5AT91_RHOCB] |
| | <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: Rhodonostoc capsulatum molisch 1907]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Capdevila, D A]] | + | [[Category: Rhodobacter capsulatus]] |
| - | [[Category: Giedroc, D P]] | + | [[Category: Capdevila DA]] |
| - | [[Category: Gonzalez-Gutierrez, G]] | + | [[Category: Giedroc DP]] |
| - | [[Category: Photosynthesis regulation]] | + | [[Category: Gonzalez-Gutierrez G]] |
| - | [[Category: Reactive sulfur species]]
| + | |
| - | [[Category: Sulfide sensor]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
| Structural highlights
Function
D5AT91_RHOCB
Publication Abstract from PubMed
Cysteine thiol-based transcriptional regulators orchestrate the coordinated regulation of redox homeostasis and other cellular processes by 'sensing' or detecting a specific redox-active molecule, which in turn activates the transcription of a specific detoxification pathway. The extent to which these sensors are truly specific in cells for a singular class of reactive small-molecule stressors, for example, reactive oxygen or sulfur species, is largely unknown. Here, we report structural and mechanistic insights into the thiol-based transcriptional repressor SqrR, which reacts exclusively with oxidized sulfur species such as persulfides, to yield a tetrasulfide bridge that inhibits DNA operator-promoter binding. Evaluation of crystallographic structures of SqrR in various derivatized states, coupled with the results of a mass spectrometry-based kinetic profiling strategy, suggest that persulfide selectivity is determined by structural frustration of the disulfide form. These findings led to the identification of an uncharacterized repressor from the bacterial pathogen Acinetobacter baumannii as a persulfide sensor.
Structural basis for persulfide-sensing specificity in a transcriptional regulator.,Capdevila DA, Walsh BJC, Zhang Y, Dietrich C, Gonzalez-Gutierrez G, Giedroc DP Nat Chem Biol. 2020 Oct 26. pii: 10.1038/s41589-020-00671-9. doi:, 10.1038/s41589-020-00671-9. PMID:33106663[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Capdevila DA, Walsh BJC, Zhang Y, Dietrich C, Gonzalez-Gutierrez G, Giedroc DP. Structural basis for persulfide-sensing specificity in a transcriptional regulator. Nat Chem Biol. 2020 Oct 26. pii: 10.1038/s41589-020-00671-9. doi:, 10.1038/s41589-020-00671-9. PMID:33106663 doi:http://dx.doi.org/10.1038/s41589-020-00671-9
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