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| | <StructureSection load='3zkc' size='340' side='right'caption='[[3zkc]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='3zkc' size='340' side='right'caption='[[3zkc]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zkc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZKC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zkc]] 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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZKC FirstGlance]. <br> |
| - | </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=3zkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zkc OCA], [https://pdbe.org/3zkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zkc RCSB], [https://www.ebi.ac.uk/pdbsum/3zkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zkc ProSAT]</span></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]] 3Å</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=3zkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zkc OCA], [https://pdbe.org/3zkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zkc RCSB], [https://www.ebi.ac.uk/pdbsum/3zkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zkc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lewis, R J]] | + | [[Category: Lewis RJ]] |
| - | [[Category: Newman, J A]] | + | [[Category: Newman JA]] |
| - | [[Category: Rodrigues, C]] | + | [[Category: Rodrigues C]] |
| - | [[Category: Biofilm]]
| + | |
| - | [[Category: Hth type transcriptional repressor]]
| + | |
| - | [[Category: Transcription-dna complex]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4]
Publication Abstract from PubMed
SinR is the master regulator that determines whether Bacillus subtilis switches from a free-living, planktonic lifestyle to form a biofilm, a community of cells attached to a surface by an extracellular matrix. Biofilms are an increasing environmental and healthcare issue, causing problems ranging from the bio-fouling of ocean-going vessels, to dental plaque, infections of the urinary tract and contamination of medical instruments such as catheters. SinR inhibits biofilm formation by repressing a number of extracellular matrix-associated operons. The activity of SinR is controlled by the SinR antagonists, SinI, SlrA and SlrR, which interact with SinR to regulate its function. We have combined isothermal titration calorimetry (ITC) and surface plasmon resonance (SPR) to determine the thermodynamic and kinetic parameters governing the protein:protein and protein:DNA interactions at the heart of this epigenetic switch. Finally, we present the crystal structure of the SinR tetramer in complex with DNA, revealing the molecular basis of base-specific DNA recognition by SinR and the mode by which SinR activity is controlled by interaction with its antagonists.
Molecular Basis of the Activity of SinR, the Master Regulator of Biofilm Formation in Bacillus subtilis.,Newman JA, Rodrigues C, Lewis RJ J Biol Chem. 2013 Feb 21. PMID:23430750[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gaur NK, Oppenheim J, Smith I. The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein. J Bacteriol. 1991 Jan;173(2):678-86. PMID:1898931
- ↑ Mandic-Mulec I, Doukhan L, Smith I. The Bacillus subtilis SinR protein is a repressor of the key sporulation gene spo0A. J Bacteriol. 1995 Aug;177(16):4619-27. PMID:7642487
- ↑ Kearns DB, Chu F, Branda SS, Kolter R, Losick R. A master regulator for biofilm formation by Bacillus subtilis. Mol Microbiol. 2005 Feb;55(3):739-49. PMID:15661000 doi:10.1111/j.1365-2958.2004.04440.x
- ↑ Kodgire P, Dixit M, Rao KK. ScoC and SinR negatively regulate epr by corepression in Bacillus subtilis. J Bacteriol. 2006 Sep;188(17):6425-8. PMID:16923912 doi:10.1128/JB.00427-06
- ↑ Newman JA, Rodrigues C, Lewis RJ. Molecular Basis of the Activity of SinR, the Master Regulator of Biofilm Formation in Bacillus subtilis. J Biol Chem. 2013 Feb 21. PMID:23430750 doi:http://dx.doi.org/10.1074/jbc.M113.455592
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