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4b9p

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Current revision

Biomass sensoring module from putative Rsgi2 protein of Clostridium thermocellum resemble family 3 carbohydrate-binding module of cellulosome

Structural highlights

4b9p is a 1 chain structure with sequence from Acetivibrio thermocellus ATCC 27405. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.182Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RSGI2_ACET2 Anti-sigma factor for SigI2. Negatively regulates SigI2 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI2 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI2.[UniProtKB:A3DBH1]

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4b9p"

@@ Line 3: / Line 3: @@
 <StructureSection load='4b9p' size='340' side='right'caption='[[4b9p]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4b9p]] 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=4B9P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B9P FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4b9p]] 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=4B9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B9P 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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.182&#8491;</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=4b9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b9p OCA], [http://pdbe.org/4b9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b9p RCSB], [http://www.ebi.ac.uk/pdbsum/4b9p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b9p 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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4b9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b9p OCA], [https://pdbe.org/4b9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b9p RCSB], [https://www.ebi.ac.uk/pdbsum/4b9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b9p ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/RSGI2_ACET2 RSGI2_ACET2] Anti-sigma factor for SigI2. Negatively regulates SigI2 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI2 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI2.[UniProtKB:A3DBH1]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Cloth]]
+[[Category: Acetivibrio thermocellus ATCC 27405]]
 [[Category: Large Structures]]
-[[Category: Bayer, E A]]
+[[Category: Bayer EA]]
-[[Category: Frolow, F]]
+[[Category: Frolow F]]
-[[Category: Lamed, R]]
+[[Category: Lamed R]]
-[[Category: Shimon, L J.W]]
+[[Category: Shimon LJW]]
-[[Category: Yaniv, O]]
+[[Category: Yaniv O]]
-[[Category: Biomass sensing system]]
-[[Category: Carbohydrate-binding protein]]
-[[Category: Cellulose]]
-[[Category: Rsgi-like protein]]

4b9p

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Current revision

Biomass sensoring module from putative Rsgi2 protein of Clostridium thermocellum resemble family 3 carbohydrate-binding module of cellulosome

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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