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| | ==Biomass sensoring modules from putative Rsgi-like proteins of Clostridium thermocellum resemble family 3 carbohydrate-binding module of cellulosome== | | ==Biomass sensoring modules from putative Rsgi-like proteins of Clostridium thermocellum resemble family 3 carbohydrate-binding module of cellulosome== |
| - | <StructureSection load='4b9c' size='340' side='right' caption='[[4b9c]], [[Resolution|resolution]] 1.17Å' scene=''> | + | <StructureSection load='4b9c' size='340' side='right'caption='[[4b9c]], [[Resolution|resolution]] 1.17Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4b9c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cloth Cloth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B9C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4b9c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_ATCC_27405 Acetivibrio thermocellus ATCC 27405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B9C 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]] 1.171Å</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=4b9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b9c OCA], [http://pdbe.org/4b9c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b9c RCSB], [http://www.ebi.ac.uk/pdbsum/4b9c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b9c ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b9c OCA], [https://pdbe.org/4b9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b9c RCSB], [https://www.ebi.ac.uk/pdbsum/4b9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b9c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/RSGI1_ACET2 RSGI1_ACET2] Anti-sigma factor for SigI1. Negatively regulates SigI1 activity through direct interaction (PubMed:20937888). Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI1 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI1 (Probable).<ref>PMID:20937888</ref> <ref>PMID:20937888</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: Cloth]] | + | [[Category: Acetivibrio thermocellus ATCC 27405]] |
| - | [[Category: Bayer, E A]] | + | [[Category: Large Structures]] |
| - | [[Category: Frolow, F]] | + | [[Category: Bayer EA]] |
| - | [[Category: Lamed, R]] | + | [[Category: Frolow F]] |
| - | [[Category: Shimon, L J.W]] | + | [[Category: Lamed R]] |
| - | [[Category: Yaniv, O]] | + | [[Category: Shimon LJW]] |
| - | [[Category: Biomass sensoring system]]
| + | [[Category: Yaniv O]] |
| - | [[Category: Carbohydrate-binding protein]]
| + | |
| Structural highlights
Function
RSGI1_ACET2 Anti-sigma factor for SigI1. Negatively regulates SigI1 activity through direct interaction (PubMed:20937888). Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI1 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI1 (Probable).[1] [2]
Publication Abstract from PubMed
The anaerobic, thermophilic, cellulosome-producing bacterium Clostridium thermocellum relies on a variety of carbohydrate-active enzymes in order to efficiently break down complex carbohydrates into utilizable simple sugars. The regulation mechanism of the cellulosomal genes was unknown until recently, when genomic analysis revealed a set of putative operons in C. thermocellum that encode sigma(I) factors (i.e. alternative sigma factors that control specialized regulon activation) and their cognate anti-sigma(I) factor (RsgI). These putative anti-sigma(I)-factor proteins have modules that are believed to be carbohydrate sensors. Three of these modules were crystallized and their three-dimensional structures were solved. The structures show a high overall degree of sequence and structural similarity to the cellulosomal family 3 carbohydrate-binding modules (CBM3s). The structures of the three carbohydrate sensors (RsgI-CBM3s) and a reference CBM3 are compared in the context of the structural determinants for the specificity of cellulose and complex carbohydrate binding. Fine structural variations among the RsgI-CBM3s appear to result in alternative substrate preferences for each of the sensors.
Fine-structural variance of family 3 carbohydrate-binding modules as extracellular biomass-sensing components of Clostridium thermocellum anti-sigma(I) factors.,Yaniv O, Fichman G, Borovok I, Shoham Y, Bayer EA, Lamed R, Shimon LJ, Frolow F Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):522-34. doi:, 10.1107/S139900471302926X. Epub 2014 Jan 31. PMID:24531486[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nataf Y, Bahari L, Kahel-Raifer H, Borovok I, Lamed R, Bayer EA, Sonenshein AL, Shoham Y. Clostridium thermocellum cellulosomal genes are regulated by extracytoplasmic polysaccharides via alternative sigma factors. Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18646-51. doi:, 10.1073/pnas.1012175107. Epub 2010 Oct 11. PMID:20937888 doi:http://dx.doi.org/10.1073/pnas.1012175107
- ↑ Nataf Y, Bahari L, Kahel-Raifer H, Borovok I, Lamed R, Bayer EA, Sonenshein AL, Shoham Y. Clostridium thermocellum cellulosomal genes are regulated by extracytoplasmic polysaccharides via alternative sigma factors. Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18646-51. doi:, 10.1073/pnas.1012175107. Epub 2010 Oct 11. PMID:20937888 doi:http://dx.doi.org/10.1073/pnas.1012175107
- ↑ Yaniv O, Fichman G, Borovok I, Shoham Y, Bayer EA, Lamed R, Shimon LJ, Frolow F. Fine-structural variance of family 3 carbohydrate-binding modules as extracellular biomass-sensing components of Clostridium thermocellum anti-sigma(I) factors. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):522-34. doi:, 10.1107/S139900471302926X. Epub 2014 Jan 31. PMID:24531486 doi:http://dx.doi.org/10.1107/S139900471302926X
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