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| [[Image:1aoh.gif|left|200px]]
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| {{Structure
| | ==SINGLE COHESIN DOMAIN FROM THE SCAFFOLDING PROTEIN CIPA OF THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME== |
| |PDB= 1aoh |SIZE=350|CAPTION= <scene name='initialview01'>1aoh</scene>, resolution 1.7Å
| | <StructureSection load='1aoh' size='340' side='right'caption='[[1aoh]], [[Resolution|resolution]] 1.70Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND=
| | <table><tr><td colspan='2'>[[1aoh]] is a 2 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=1AOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOH FirstGlance]. <br> |
| |ACTIVITY=
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| |GENE= LACI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 Clostridium thermocellum]) | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aoh OCA], [https://pdbe.org/1aoh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aoh RCSB], [https://www.ebi.ac.uk/pdbsum/1aoh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aoh ProSAT]</span></td></tr> |
| }}
| | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/CIPA_ACET2 CIPA_ACET2] Acts as a scaffolding protein in the cellulosome. It promotes binding of cellulose to the catalytic domains of the cellulolytic enzymes. |
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ao/1aoh_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1aoh ConSurf]. |
| | <div style="clear:both"></div> |
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| '''SINGLE COHESIN DOMAIN FROM THE SCAFFOLDING PROTEIN CIPA OF THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME'''
| | ==See Also== |
| | | *[[Cellulosome scaffolding protein 3D structures|Cellulosome scaffolding protein 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| The quaternary organization of the cellulosome, a multi-enzymatic extracellular complex produced by cellulolytic bacteria, depends on specific interactions between dockerin domains, double EF-hand subunits carried by the catalytic components, and cohesin domains, individual receptor subunits linearly arranged within a non-catalytic scaffolding polypeptide. Cohesin-dockerin complexes with distinct specificities are also thought to mediate the attachment of cellulosomes to the cell membrane.We report here the crystal structure of a single cohesin domain from the scaffolding protein of Clostridium thermocellum. The cohesin domain folds into a nine-stranded beta-sandwich with an overall "jelly roll" topology, similar to that observed in bacterial cellulose-binding domains. Surface-exposed patches of conserved residues promote extensive intermolecular contacts in the crystal, and suggest a possible binding target for the EF-hand pair of the cognate dockerin domain. Comparative studies of cohesin domains indicate that, in spite of low sequence similarities and different functional roles, all cohesin domains share a common nine-stranded beta-barrel fold stabilized by a conserved hydrophobic core.The formation of stable cohesin-dockerin complexes requires the presence of Ca2+. However, the structure of the cohesin domain reported here reveals no obvious Ca2+-binding site, and previous experiments have failed to detect high affinity binding of Ca2+ to the unliganded dockerin domain of endoglucanase CelD. Based on structural and biochemical evidence, we propose a model of the cohesin-dockerin complex in which the dockerin domain requires complexation with its cohesin partner for protein stability and high-affinity Ca2+ binding.
| | [[Category: Acetivibrio thermocellus ATCC 27405]] |
| | | [[Category: Large Structures]] |
| ==About this Structure==
| | [[Category: Alzari PM]] |
| 1AOH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOH OCA].
| | [[Category: Tavares G]] |
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| ==Reference==
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| The crystal structure of a type I cohesin domain at 1.7 A resolution., Tavares GA, Beguin P, Alzari PM, J Mol Biol. 1997 Oct 31;273(3):701-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9402065 9402065]
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| [[Category: Clostridium thermocellum]] | |
| [[Category: Single protein]] | |
| [[Category: Alzari, P M.]] | |
| [[Category: Tavares, G.]] | |
| [[Category: b-barrel]]
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| [[Category: cellulose degradation]]
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| [[Category: cellulosome subunit]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:19 2008''
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