4p5h

Structure of Clostridium perfringens Enterotoxin with a peptide derived from a modified version of ECL-2 of Claudin 2

spinqualitylabelsall models 4p5h, resolution 3.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4p5h is a 30 chain structure. This structure supersedes the now removed PDB entry 3zj3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Function [CLD2_MOUSE] Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. [ELTB_CLOPF] This enterotoxin is responsible for many cases of a mild type of food poisoning. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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