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New page: left|200px<br /><applet load="1g1k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g1k, resolution 2.00Å" /> '''COHESIN MODULE FROM ...
 
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[[Image:1g1k.gif|left|200px]]<br /><applet load="1g1k" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1g1k, resolution 2.00&Aring;" />
'''COHESIN MODULE FROM THE CELLULOSOME OF CLOSTRIDIUM CELLULOLYTICUM'''<br />


==Overview==
==COHESIN MODULE FROM THE CELLULOSOME OF CLOSTRIDIUM CELLULOLYTICUM==
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.
<StructureSection load='1g1k' size='340' side='right'caption='[[1g1k]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
1G1K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G1K OCA].  
</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>
 
<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>
==Reference==
</table>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11080455 11080455]
== Function ==
[[Category: Clostridium cellulolyticum]]
[https://www.uniprot.org/uniprot/Q45996_9FIRM Q45996_9FIRM]
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Category: Belaich, A.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Belaich, J.P.]]
Check<jmol>
[[Category: Cambillau, C.]]
  <jmolCheckbox>
[[Category: Fierobe, H.P.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/1g1k_consurf.spt"</scriptWhenChecked>
[[Category: Henrissat, B.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Spinelli, S.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: beta -barrel]]
  </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=1g1k ConSurf].
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:40:03 2007''
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ruminiclostridium cellulolyticum]]
[[Category: Belaich A]]
[[Category: Belaich J-P]]
[[Category: Cambillau C]]
[[Category: Fierobe H-P]]
[[Category: Henrissat B]]
[[Category: Spinelli S]]
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