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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ozn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens] and [https://en.wikipedia.org/wiki/Clostridium_perfringens_ATCC_13124 Clostridium perfringens ATCC 13124]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OZN FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ozn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens] and [https://en.wikipedia.org/wiki/Clostridium_perfringens_ATCC_13124 Clostridium perfringens ATCC 13124]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OZN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=2ozn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ozn OCA], [https://pdbe.org/2ozn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ozn RCSB], [https://www.ebi.ac.uk/pdbsum/2ozn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ozn ProSAT], [https://www.topsan.org/Proteins/BSGI/2ozn TOPSAN]</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=2ozn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ozn OCA], [https://pdbe.org/2ozn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ozn RCSB], [https://www.ebi.ac.uk/pdbsum/2ozn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ozn ProSAT], [https://www.topsan.org/Proteins/BSGI/2ozn TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/NAGH_CLOPE NAGH_CLOPE] Putative virulence factor which is likely to act on connective tissue during gas gangrene.
[https://www.uniprot.org/uniprot/NAGH_CLOPE NAGH_CLOPE] Putative virulence factor which is likely to act on connective tissue during gas gangrene.
<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 2ozn" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
*[[O-GlcNAcase|O-GlcNAcase]]
*[[O-GlcNAcase|O-GlcNAcase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

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