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| ==Solution Structure of the C-terminal multimerization domain of the master biofilm-regulator SinR from Bacillus subtilis== | | ==Solution Structure of the C-terminal multimerization domain of the master biofilm-regulator SinR from Bacillus subtilis== |
| <StructureSection load='5tn2' size='340' side='right'caption='[[5tn2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | | <StructureSection load='5tn2' size='340' side='right'caption='[[5tn2]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5tn2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TN2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TN2 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5tn2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TN2 FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tn0|5tn0]], [[5tmx|5tmx]]</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sinR, flaD, sin, BSU24610 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=5tn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tn2 OCA], [https://pdbe.org/5tn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tn2 RCSB], [https://www.ebi.ac.uk/pdbsum/5tn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tn2 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=5tn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tn2 OCA], [http://pdbe.org/5tn2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tn2 RCSB], [http://www.ebi.ac.uk/pdbsum/5tn2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tn2 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/SINR_BACSU SINR_BACSU]] Negative as well as positive regulator of alternate developmental processes that are induced at the end of vegetative growth in response to nutrient depletion. Binds to the alkaline protease (aprE) gene at two sites. Also acts as a repressor of the key sporulation gene spo0A. Negatively regulates transcription of the eps operon, which is responsible for the biosynthesis of an exopolysaccharide involved in biofilm formation; therefore it could govern the transition between a state in which bacteria swim or swarm and a state in which bacteria assemble into multicellular communities. Acts with Hpr as a corepressor of epr expression. Also negatively regulates transcription of the lutABC operon, which is required for lactate utilization. Repressor activity is regulated by SinI.<ref>PMID:1898931</ref> <ref>PMID:7642487</ref> <ref>PMID:15661000</ref> <ref>PMID:16923912</ref> | | [https://www.uniprot.org/uniprot/SINR_BACSU SINR_BACSU] Negative as well as positive regulator of alternate developmental processes that are induced at the end of vegetative growth in response to nutrient depletion. Binds to the alkaline protease (aprE) gene at two sites. Also acts as a repressor of the key sporulation gene spo0A. Negatively regulates transcription of the eps operon, which is responsible for the biosynthesis of an exopolysaccharide involved in biofilm formation; therefore it could govern the transition between a state in which bacteria swim or swarm and a state in which bacteria assemble into multicellular communities. Acts with Hpr as a corepressor of epr expression. Also negatively regulates transcription of the lutABC operon, which is required for lactate utilization. Repressor activity is regulated by SinI.<ref>PMID:1898931</ref> <ref>PMID:7642487</ref> <ref>PMID:15661000</ref> <ref>PMID:16923912</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Bacteria have developed numerous protection strategies to ensure survival in harsh environments, with perhaps the most robust method being the formation of a protective biofilm. In biofilms, bacterial cells are embedded within a matrix that is composed of a complex mixture of polysaccharides, proteins and DNA. The Gram-positive bacterium Bacillus subtilis has become a model organism for studying regulatory networks directing biofilm formation. The phenotypic transition from a planktonic to biofilm state is regulated by the activity of the transcriptional repressor, SinR, and its inactivation by its primary antagonist, SinI. In this work, we present the first full-length structural model of tetrameric SinR using a hybrid approach combining high-resolution solution NMR, chemical crosslinking, mass spectrometry, and molecular docking. We also present the solution NMR structure of the antagonist SinI dimer, and probe the mechanism behind the SinR-SinI interaction using a combination of biochemical and biophysical techniques. As a result of these findings, we propose that SinI utilizes a residue replacement mechanism to block SinR multimerization, resulting in diminished DNA binding and concomitant decreased repressor activity. Finally, we provide an evidence-based mechanism that confirms how disruption of the SinR tetramer by SinI regulates gene expression.
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| The Solution Structures and Interaction of SinR and SinI: Elucidating the Mechanism of Action of the Master Regulator Switch for Biofilm Formation in Bacillus subtilis.,Milton ME, Draughn GL, Bobay BG, Stowe SD, Olson AL, Feldmann EA, Thompson RJ, Myers KH, Santoro MT, Kearns DB, Cavanagh J J Mol Biol. 2019 Sep 4. pii: S0022-2836(19)30543-1. doi:, 10.1016/j.jmb.2019.08.019. PMID:31493408<ref>PMID:31493408</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5tn2" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacsu]] | | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Bobay, B G]] | | [[Category: Bobay BG]] |
| [[Category: Cavanagh, J]] | | [[Category: Cavanagh J]] |
| [[Category: Draughn, G L]] | | [[Category: Draughn GL]] |
| [[Category: Stowe, S D]] | | [[Category: Stowe SD]] |
| [[Category: Thompson, R J]] | | [[Category: Thompson RJ]] |
| [[Category: Biofilm formation]]
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| [[Category: Multimerization domain]]
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| [[Category: Transcription]]
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