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<StructureSection load='1ca1' size='340' side='right'caption='[[1ca1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1ca1' size='340' side='right'caption='[[1ca1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ca1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CA1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ca1]] 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=1CA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CA1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1ca1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ca1 OCA], [https://pdbe.org/1ca1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ca1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ca1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ca1 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=1ca1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ca1 OCA], [https://pdbe.org/1ca1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ca1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ca1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ca1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PHLC1_CLOPE PHLC1_CLOPE]] Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Constitutes an essential virulence factor in gas gangrene. Binds to eukaryotic membranes where it hydrolyzes both phosphatidylcholine and sphingomyelin. The diacylglycerol produced can activate both the arachidonic acid pathway, leading to modulation of the inflammatory response cascade and thrombosis, and protein kinase C, leading to activation of eukaryotic phospholipases and further membrane damage. Acts on human and mouse erythrocytes, but not on rabbit or horse erythrocytes.  
[https://www.uniprot.org/uniprot/PHLC1_CLOPE PHLC1_CLOPE] Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Constitutes an essential virulence factor in gas gangrene. Binds to eukaryotic membranes where it hydrolyzes both phosphatidylcholine and sphingomyelin. The diacylglycerol produced can activate both the arachidonic acid pathway, leading to modulation of the inflammatory response cascade and thrombosis, and protein kinase C, leading to activation of eukaryotic phospholipases and further membrane damage. Acts on human and mouse erythrocytes, but not on rabbit or horse erythrocytes.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ca1 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ca1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Clostridium perfringens alpha-toxin is the key virulence determinant in gas gangrene and has also been implicated in the pathogenesis of sudden death syndrome in young animals. The toxin is a 370-residue, zinc metalloenzyme that has phospholipase C activity, and can bind to membranes in the presence of calcium. The crystal structure of the enzyme reveals a two-domain protein. The N-terminal domain shows an anticipated structural similarity to Bacillus cereus phosphatidylcholine-specific phospholipase C (PC-PLC). The C-terminal domain shows a strong structural analogy to eukaryotic calcium-binding C2 domains. We believe this is the first example of such a domain in prokaryotes. This type of domain has been found to act as a phospholipid and/or calcium-binding domain in intracellular second messenger proteins and, interestingly, these pathways are perturbed in cells treated with alpha-toxin. Finally, a possible mechanism for alpha-toxin attack on membrane-packed phospholipid is described, which rationalizes its toxicity when compared to other, non-haemolytic, but homologous phospholipases C.
Structure of the key toxin in gas gangrene.,Naylor CE, Eaton JT, Howells A, Justin N, Moss DS, Titball RW, Basak AK Nat Struct Biol. 1998 Aug;5(8):738-46. PMID:9699639<ref>PMID:9699639</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ca1" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hemolysin 3D structures|Hemolysin 3D structures]]
*[[Hemolysin 3D structures|Hemolysin 3D structures]]
*[[Phospholipase C|Phospholipase C]]
*[[Phospholipase C|Phospholipase C]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clostridium perfringens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phospholipase C]]
[[Category: Basak AK]]
[[Category: Basak, A K]]
[[Category: Naylor CE]]
[[Category: Naylor, C E]]
[[Category: Titball RW]]
[[Category: Titball, R W]]
[[Category: C2 domain]]
[[Category: Ca and membrane binding]]
[[Category: Gangrene determinant]]
[[Category: Hydrolase]]
[[Category: Zinc phospholipase c]]

Latest revision as of 05:57, 3 April 2024

ALPHA-TOXIN FROM CLOSTRIDIUM PERFRINGENS

1ca1, resolution 1.90Å

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