1g1k: Difference between revisions

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<StructureSection load='1g1k' size='340' side='right'caption='[[1g1k]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1g1k' size='340' side='right'caption='[[1g1k]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1g1k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35319 Atcc 35319]. 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>
<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>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aoh|1aoh]], [[1anu|1anu]]</div></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]] 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>
<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>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q45996_9FIRM Q45996_9FIRM]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:11080455<ref>PMID:11080455</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1g1k" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 35319]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Belaich, A]]
[[Category: Ruminiclostridium cellulolyticum]]
[[Category: Belaich, J P]]
[[Category: Belaich A]]
[[Category: Cambillau, C]]
[[Category: Belaich J-P]]
[[Category: Fierobe, H P]]
[[Category: Cambillau C]]
[[Category: Henrissat, B]]
[[Category: Fierobe H-P]]
[[Category: Spinelli, S]]
[[Category: Henrissat B]]
[[Category: Beta -barrel]]
[[Category: Spinelli S]]
[[Category: Structural protein]]

Latest revision as of 07:21, 7 February 2024

COHESIN MODULE FROM THE CELLULOSOME OF CLOSTRIDIUM CELLULOLYTICUM

1g1k, resolution 2.00Å

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