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1g1k

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[[Image:1g1k.gif|left|200px]]
 
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{{Structure
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==COHESIN MODULE FROM THE CELLULOSOME OF CLOSTRIDIUM CELLULOLYTICUM==
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|PDB= 1g1k |SIZE=350|CAPTION= <scene name='initialview01'>1g1k</scene>, resolution 2.00&Aring;
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<StructureSection load='1g1k' size='340' side='right'caption='[[1g1k]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1g1k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminiclostridium_cellulolyticum Ruminiclostridium cellulolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1K FirstGlance]. <br>
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|ACTIVITY=
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</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&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1k OCA], [https://pdbe.org/1g1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1k RCSB], [https://www.ebi.ac.uk/pdbsum/1g1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1k ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''COHESIN MODULE FROM THE CELLULOSOME OF CLOSTRIDIUM CELLULOLYTICUM'''
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[https://www.uniprot.org/uniprot/Q45996_9FIRM Q45996_9FIRM]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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In the assembly of the Clostridium cellulolyticum cellulosome, the multiple cohesin modules of the scaffolding protein CipC serve as receptors for cellulolytic enzymes which bear a dockerin module. The X-ray structure of a type I C. cellulolyticum cohesin module (Cc-cohesin) has been solved using molecular replacement, and refined at 2.0 A resolution. Despite a rather low sequence identity of 32 %, this module has a fold close to those of the two Clostridium thermocellum cohesin (Ct-cohesin) modules whose 3D structures have been determined previously. Cc-cohesin forms a dimer in the crystal, as do the two Ct-cohesins. We show here that the dimer exists in solution and that addition of dockerin-containing proteins dissociates the dimer. This suggests that the dimerization interface and the cohesin/dockerin interface may overlap. The nature of the overall surface and of the dimer interface of Cc-cohesin differ notably from those of the Ct-cohesin modules, being much less polar, and this may explain the species specificity observed in the cohesin/dockerin interaction of C. cellulolyticum and C. thermocellum. We have produced a topology model of a C. cellulolyticum dockerin and of a Cc-cohesin/dockerin complex using homology modeling and available biochemical data. Our model suggests that a special residue pair, already identified in dockerin sequences, is located at the center of the cohesin surface putatively interacting with the dockerin.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/1g1k_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1G1K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1K OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</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=1g1k ConSurf].
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Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition., Spinelli S, Fierobe HP, Belaich A, Belaich JP, Henrissat B, Cambillau C, J Mol Biol. 2000 Nov 24;304(2):189-200. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080455 11080455]
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<div style="clear:both"></div>
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[[Category: Clostridium cellulolyticum]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Belaich, A.]]
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[[Category: Large Structures]]
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[[Category: Belaich, J P.]]
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[[Category: Ruminiclostridium cellulolyticum]]
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[[Category: Cambillau, C.]]
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[[Category: Belaich A]]
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[[Category: Fierobe, H P.]]
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[[Category: Belaich J-P]]
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[[Category: Henrissat, B.]]
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[[Category: Cambillau C]]
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[[Category: Spinelli, S.]]
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[[Category: Fierobe H-P]]
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[[Category: beta -barrel]]
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[[Category: Henrissat B]]
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[[Category: Spinelli S]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:54 2008''
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Current revision

COHESIN MODULE FROM THE CELLULOSOME OF CLOSTRIDIUM CELLULOLYTICUM

PDB ID 1g1k

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