1g1k

<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>

</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>

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== 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>

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== References ==

<references/>

[[Category: Atcc 35319]]

[[Category: Belaich, A]]

[[Category: Belaich, J P]]

[[Category: Cambillau, C]]

[[Category: Fierobe, H P]]

[[Category: Henrissat, B]]

[[Category: Spinelli, S]]

[[Category: Structural protein]]