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| | <StructureSection load='6qe7' size='340' side='right'caption='[[6qe7]], [[Resolution|resolution]] 2.06Å' scene=''> | | <StructureSection load='6qe7' size='340' side='right'caption='[[6qe7]], [[Resolution|resolution]] 2.06Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qe7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_(viljoen_et_al._1926)_yutin_and_galperin_2013 "ruminiclostridium thermocellum" (viljoen et al. 1926) yutin and galperin 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QE7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qe7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QE7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.06Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qdi|6qdi]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rsgI3, Cthe_0316 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 "Ruminiclostridium thermocellum" (Viljoen et al. 1926) Yutin and Galperin 2013])</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=6qe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qe7 OCA], [https://pdbe.org/6qe7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qe7 RCSB], [https://www.ebi.ac.uk/pdbsum/6qe7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qe7 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=6qe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qe7 OCA], [http://pdbe.org/6qe7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qe7 RCSB], [http://www.ebi.ac.uk/pdbsum/6qe7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qe7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RSGI3_CLOTH RSGI3_CLOTH]] Anti-sigma factor for SigI3. Negatively regulates SigI3 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI3 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI3.[UniProtKB:A3DBH1] | + | [https://www.uniprot.org/uniprot/RSGI3_ACET2 RSGI3_ACET2] Anti-sigma factor for SigI3. Negatively regulates SigI3 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI3 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI3.[UniProtKB:A3DBH1] |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Cellulolytic clostridia use a highly efficient cellulosome system to degrade polysaccharides. To regulate genes encoding enzymes of the multi-enzyme cellulosome complex, certain clostridia contain alternative sigma I (sigma(I) ) factors that have cognate membrane associated anti-sigma(I) factors (RsgIs) which act as polysaccharide sensors. In this work, we analyzed the structure-function relationship of the extracellular sensory elements of Clostridium (Ruminiclostridium) thermocellum and Clostridium clariflavum (RsgI3 and RsgI4, respectively). These elements were selected for comparison as each comprised two tandem PA14-superfamily motifs. The X-ray structures of the PA14 modular dyads from the two bactrerial species were determined, both of which showed a high degree of structural and sequence similarity, although their binding preferences differed. Bioinformatic approaches indicated that the DNA sequence of promoter of sigI/rsgI operons represents a strong signature which helps differentiate binding specificity of the structurally similar modules. The sigma(I4) -dependent C. clariflavum promoter sequence correlates with binding of RsgI4_PA14 to xylan and was identified in genes encoding xylanases, whereas the sigma(I3) -dependent C. thermocellum promoter sequence correlates with RsgI3_PA14 binding to pectin and regulates pectin degradation-related genes. Structural similarity between clostridial PA14 dyads to PA14-containing proteins in yeast helped identify another crucial signature element: the Calcium Binding Loop 2 (CBL2), which governs binding specificity. Variations in the five amino acids that constitute this loop distinguishes the pectin versus xylan specificities. We propose that the first module (PA14(A) ) is dominant in directing the binding to the ligand in both bacteria. The two X-ray structures of the different PA14 dyads represent the first reported structures of tandem PA14 modules. This article is protected by copyright. All rights reserved.
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| - | Distinctive ligand-binding specificities of tandem PA14 biomass-sensory elements from Clostridium thermocellum and Clostridium clariflavum.,Rozman Grinberg I, Yaniv O, Ortiz de Ora L, Munoz-Gutierrez I, Hershko A, Livnah O, Bayer EA, Borovok I, Frolow F, Lamed R, Voronov-Goldman M Proteins. 2019 Jun 4. doi: 10.1002/prot.25753. PMID:31162722<ref>PMID:31162722</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 6qe7" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Acetivibrio thermocellus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bayer, E A]] | + | [[Category: Bayer EA]] |
| - | [[Category: Livnah, O]] | + | [[Category: Livnah O]] |
| - | [[Category: Voronov, M]] | + | [[Category: Voronov M]] |
| - | [[Category: Anti-sigma factor]]
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| - | [[Category: Biomass sensing]]
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| - | [[Category: Cellulosome]]
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| - | [[Category: Rsgi]]
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| - | [[Category: Sigi]]
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| - | [[Category: Sigma factor]]
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| - | [[Category: Sugar binding protein]]
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