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==Solution structure of a dockerin-containing modular pair from a family 84 glycoside hydrolase==
<StructureSection load='2jnk' size='340' side='right'caption='[[2jnk]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jnk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JNK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jnk OCA], [https://pdbe.org/2jnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jnk RCSB], [https://www.ebi.ac.uk/pdbsum/2jnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jnk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NAGH_CLOPE NAGH_CLOPE] Putative virulence factor which is likely to act on connective tissue during gas gangrene.
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== Publication Abstract from PubMed ==
The genome of the opportunistic pathogen Clostridium perfringens encodes a large number of secreted glycoside hydrolases. Their predicted activities indicate that they are involved in the breakdown of complex carbohydrates and other glycans found in the mucosal layer of the human gastrointestinal tract, within the extracellular matrix, and on the surface of host cells. One such group of these enzymes is the family 84 glycoside hydrolases, which has predicted hyaluronidase activity and comprises five members [C. perfringens glycoside hydrolase family 84 (CpGH84) A-E]. The first identified member, CpGH84A, corresponds to the mu-toxin whose modular architecture includes an N-terminal catalytic domain, four family 32 carbohydrate-binding modules, three FIVAR modules of unknown function, and a C-terminal putative calcium-binding module. Here, we report the solution NMR structure of the C-terminal modular pair from the mu-toxin. The three-helix bundle FIVAR module displays structural homology to a heparin-binding module within the N-terminal of the a C protein from group B Streptoccocus. The C-terminal module has a typical calcium-binding dockerin fold comprising two anti-parallel helices that form a planar face with EF-hand calcium-binding loops at opposite ends of the module. The size of the helical face of the mu-toxin dockerin module is approximately equal to the planar region recently identified on the surface of a cohesin-like X82 module of CpGH84C. Size-exclusion chromatography and heteronuclear NMR-based chemical shift mapping studies indicate that the helical face of the dockerin module recognizes the CpGH84C X82 module. These studies represent the structural characterization of a noncellulolytic dockerin module and its interaction with a cohesin-like X82 module. Dockerin/X82-mediated enzyme complexes may have important implications in the pathogenic properties of C. perfringens.

The solution structure of the C-terminal modular pair from Clostridium perfringens mu-toxin reveals a noncellulosomal dockerin module.,Chitayat S, Adams JJ, Furness HS, Bayer EA, Smith SP J Mol Biol. 2008 Sep 19;381(5):1202-12. Epub 2008 Jun 24. PMID:18602403<ref>PMID:18602403</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2jnk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Hyaluronidase 3D structures|Hyaluronidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium perfringens]]
[[Category: Large Structures]]
[[Category: Adams JJ]]
[[Category: Bayer EA]]
[[Category: Chitayat S]]
[[Category: Smith SP]]