2wy6

From Proteopedia

(Difference between revisions)

Current revision

Clostridium perfringens alpha-toxin strain NCTC8237 mutant T74I

Structural highlights

2wy6 is a 3 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHLC_CLOP1 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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The alpha-toxin produced by Clostridium perfringens is one of the best-studied examples of a toxic phospholipase C. In this study, a nontoxic mutant protein from C. perfringens strain NCTC8237 in which Thr74 is substituted by isoleucine (T74I) has been characterized and is compared with the toxic wild-type protein. Thr74 is part of an exposed loop at the proposed membrane-interfacing surface of the toxin. The mutant protein had markedly reduced cytotoxic and myotoxic activities. However, this substitution did not significantly affect the catalytic activity towards water-soluble substrate or the overall three-dimensional structure of the protein. The data support the proposed role of the 70-90 loop in the recognition of membrane phospholipids. These findings also provide key evidence in support of the hypothesis that the hydrolysis of both phosphatidylcholine and sphingomyelin are required for the cytolytic and toxic activity of phospholipases.

Comparison of a nontoxic variant of Clostridium perfringens alpha-toxin with the toxic wild-type strain.,Vachieri SG, Clark GC, Alape-Giron A, Flores-Diaz M, Justin N, Naylor CE, Titball RW, Basak AK Acta Crystallogr D Biol Crystallogr. 2010 Oct;66(Pt 10):1067-74. Epub 2010, Sep 18. PMID:20944240^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Vachieri SG, Clark GC, Alape-Giron A, Flores-Diaz M, Justin N, Naylor CE, Titball RW, Basak AK. Comparison of a nontoxic variant of Clostridium perfringens alpha-toxin with the toxic wild-type strain. Acta Crystallogr D Biol Crystallogr. 2010 Oct;66(Pt 10):1067-74. Epub 2010, Sep 18. PMID:20944240 doi:10.1107/S090744491003369X

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wy6"

Categories: Clostridium perfringens | Large Structures | Basak AK | Naylor CE | Vachieri SG

@@ Line 1: / Line 1: @@
-==CLOSTRIDIUM PERFRINGENS ALPHA-TOXIN STRAIN NCTC8237 MUTANT T74I==
-<StructureSection load='2wy6' size='340' side='right' caption='[[2wy6]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+==Clostridium perfringens alpha-toxin strain NCTC8237 mutant T74I==
+<StructureSection load='2wy6' size='340' side='right'caption='[[2wy6]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wy6]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WY6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wy6]] is a 3 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=2WY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WY6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 3.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qm6|1qm6]], [[2wxt|2wxt]], [[1qmd|1qmd]], [[2wxu|2wxu]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] </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=2wy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wy6 OCA], [https://pdbe.org/2wy6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wy6 RCSB], [https://www.ebi.ac.uk/pdbsum/2wy6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wy6 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wy6 OCA], [http://pdbe.org/2wy6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wy6 RCSB], [http://www.ebi.ac.uk/pdbsum/2wy6 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PHLC_CLOP1 PHLC_CLOP1]] 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/PHLC_CLOP1 PHLC_CLOP1] 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wy/2wy6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wy/2wy6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Hemolysin|Hemolysin]]
+*[[Hemolysin 3D structures|Hemolysin 3D structures]]
 *[[Phospholipase C|Phospholipase C]]
 == References ==
@@ Line 37: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus perfringens veillon and zuber 1898]]
+[[Category: Clostridium perfringens]]
-[[Category: Phospholipase C]]
+[[Category: Large Structures]]
-[[Category: Basak, A K]]
+[[Category: Basak AK]]
-[[Category: Naylor, C E]]
+[[Category: Naylor CE]]
-[[Category: Vachieri, S G]]
+[[Category: Vachieri SG]]
-[[Category: C2 domain]]
-[[Category: Cytolysis]]
-[[Category: Gangrene determinant]]
-[[Category: Hemolysis]]
-[[Category: Hydrolase]]
-[[Category: Membrane binding]]
-[[Category: Virulence]]

2wy6

From Proteopedia

Current revision

Clostridium perfringens alpha-toxin strain NCTC8237 mutant T74I

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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