3am2: Difference between revisions
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<StructureSection load='3am2' size='340' side='right'caption='[[3am2]], [[Resolution|resolution]] 2.51Å' scene=''> | <StructureSection load='3am2' size='340' side='right'caption='[[3am2]], [[Resolution|resolution]] 2.51Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3am2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3am2]] 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=3AM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AM2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=3am2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3am2 OCA], [https://pdbe.org/3am2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3am2 RCSB], [https://www.ebi.ac.uk/pdbsum/3am2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3am2 ProSAT]</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=3am2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3am2 OCA], [https://pdbe.org/3am2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3am2 RCSB], [https://www.ebi.ac.uk/pdbsum/3am2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3am2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Clostridium perfringens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Abe | [[Category: Abe H]] | ||
[[Category: Fukui | [[Category: Fukui A]] | ||
[[Category: Horiguchi | [[Category: Horiguchi Y]] | ||
[[Category: Kamitani | [[Category: Kamitani S]] | ||
[[Category: Kimura | [[Category: Kimura J]] | ||
[[Category: Kitadokoro | [[Category: Kitadokoro K]] | ||
[[Category: Nishimura | [[Category: Nishimura K]] | ||
Latest revision as of 18:48, 4 October 2023
Clostridium perfringens enterotoxinClostridium perfringens enterotoxin
Structural highlights
FunctionELTB_CLOPF This enterotoxin is responsible for many cases of a mild type of food poisoning. Publication Abstract from PubMedClostridium perfringens enterotoxin (CPE) is a cause of food poisoning and is considered a pore-forming toxin, which damages target cells by disrupting the selective permeability of the plasma membrane. However, the pore-forming mechanism and the structural characteristics of the pores are not well documented. Here, we present the structure of CPE determined by x-ray crystallography at 2.0 A. The overall structure of CPE displays an elongated shape, composed of three distinct domains, I, II, and III. Domain I corresponds to the region that was formerly referred to as C-CPE, which is responsible for binding to the specific receptor claudin. Domains II and III comprise a characteristic module, which resembles those of beta-pore-forming toxins such as aerolysin, C. perfringens epsilon-toxin, and Laetiporus sulfureus hemolytic pore-forming lectin. The module is mainly made up of beta-strands, two of which span its entire length. Domain II and domain III have three short beta-strands each, by which they are distinguished. In addition, domain II has an alpha-helix lying on the beta-strands. The sequence of amino acids composing the alpha-helix and preceding beta-strand demonstrates an alternating pattern of hydrophobic residues that is characteristic of transmembrane domains forming beta-barrel-made pores. These structural features imply that CPE is a beta-pore-forming toxin. We also hypothesize that the transmembrane domain is inserted into the membrane upon the buckling of the two long beta-strands spanning the module, a mechanism analogous to that of the cholesterol-dependent cytolysins. Crystal Structure of Clostridium perfringens Enterotoxin Displays Features of {beta}-Pore-forming Toxins.,Kitadokoro K, Nishimura K, Kamitani S, Fukui-Miyazaki A, Toshima H, Abe H, Kamata Y, Sugita-Konishi Y, Yamamoto S, Karatani H, Horiguchi Y J Biol Chem. 2011 Jun 3;286(22):19549-55. Epub 2011 Apr 12. PMID:21489981[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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