View source for 3zix


==Clostridium perfringens Enterotoxin with the N-terminal 37 residues deleted==
<StructureSection load='3zix' size='340' side='right'caption='[[3zix]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zix]] is a 6 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=3ZIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZIX 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</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=3zix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zix OCA], [https://pdbe.org/3zix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zix RCSB], [https://www.ebi.ac.uk/pdbsum/3zix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zix ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ELTB_CLOPF ELTB_CLOPF] This enterotoxin is responsible for many cases of a mild type of food poisoning.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CPE (Clostridium perfringens enterotoxin) is the major virulence determinant for C. perfringens type A food poisoning, the second most common bacterial food-borne illness in the UK and USA. After binding to its receptors, which include particular human claudins, the toxin forms pores in the cell membrane. The mature pore apparently contains a hexamer of CPE, claudin and, possibly, occludin. The combination of high binding specificity with cytotoxicity has resulted in CPE being investigated, with some success, as a targeted cytotoxic agent for oncotherapy. In this paper, we present the X-ray crystallographic structure of CPE in complex with a peptide derived from extracellular loop 2 of a modified, CPE binding Claudin-2, together with high-resolution native and pore-formation mutant structures. Our structure provides the first atomic resolution data on any part of a claudin molecule and reveals that claudin's CPE binding fingerprint (NPLVP), is in a tight turn conformation and binds, as expected, in CPE's C-terminal claudin binding groove. The leucine and valine residues insert into the binding groove while the first residue, asparagine, tethers the peptide via an interaction with CPE's aspartate 225 and the two prolines are required to maintain the tight turn conformation. Understanding the structural basis of the contribution these residues make to binding will aid in engineering CPE to target tumour cells.

Structure of a C. perfringens Enterotoxin mutant in Complex with a Modified Claudin-2 Extracellular Loop 2.,Yelland TS, Naylor CE, Bagoban T, Savva CG, Moss DS, McClane BA, Blasig IE, Popoff M, Basak AK J Mol Biol. 2014 Jul 11. pii: S0022-2836(14)00329-5. doi:, 10.1016/j.jmb.2014.07.001. PMID:25020226<ref>PMID:25020226</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zix" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium perfringens]]
[[Category: Large Structures]]
[[Category: Basak AK]]
[[Category: Naylor CE]]
[[Category: Savva CG]]
[[Category: Yelland T]]