View source for 2vo8


==Cohesin module from Clostridium perfringens ATCC13124 family 33 glycoside hydrolase.==
<StructureSection load='2vo8' size='340' side='right'caption='[[2vo8]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vo8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VO8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#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=2vo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vo8 OCA], [https://pdbe.org/2vo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vo8 RCSB], [https://www.ebi.ac.uk/pdbsum/2vo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vo8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H2YT71_CLOP1 A0A0H2YT71_CLOP1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The virulent properties of the common human and livestock pathogen Clostridium perfringens are attributable to a formidable battery of toxins. Among these are a number of large and highly modular carbohydrate-active enzymes, including the mu-toxin and sialidases, whose catalytic properties are consistent with degradation of the mucosal layer of the human gut, glycosaminoglycans, and other cellular glycans found throughout the body. The conservation of noncatalytic ancillary modules among these enzymes suggests they make significant contributions to the overall functionality of the toxins. Here, we describe the structural basis of an ultra-tight interaction (K(a) = 1.44 x 10(11) M(-1)) between the X82 and dockerin modules, which are found throughout numerous C. perfringens carbohydrate-active enzymes. Extensive hydrogen-bonding and van der Waals contacts between the X82 and dockerin modules give rise to the observed high affinity. The mu-toxin dockerin module in this complex is positioned approximately 180 degrees relative to the orientation of the dockerin modules on the cohesin module surface within cellulolytic complexes. These observations represent a unique property of these clostridial toxins whereby they can associate into large, noncovalent multitoxin complexes that allow potentiation of the activities of the individual toxins by combining complementary toxin specificities.

Structural basis of Clostridium perfringens toxin complex formation.,Adams JJ, Gregg K, Bayer EA, Boraston AB, Smith SP Proc Natl Acad Sci U S A. 2008 Aug 26;105(34):12194-9. Epub 2008 Aug 20. PMID:18716000<ref>PMID:18716000</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2vo8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Clostridium perfringens]]
[[Category: Large Structures]]
[[Category: Adams JJ]]
[[Category: Bayer EA]]
[[Category: Boraston AB]]
[[Category: Gregg K]]
[[Category: Smith SP]]