1kho

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{{STRUCTURE_1kho| PDB=1kho | SCENE= }}
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===Crystal Structure Analysis of Clostridium perfringens alpha-Toxin Isolated from Avian Strain SWCP===
===Crystal Structure Analysis of Clostridium perfringens alpha-Toxin Isolated from Avian Strain SWCP===
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{{ABSTRACT_PUBMED_12009886}}
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==Function==
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[[http://www.uniprot.org/uniprot/PHLC_CLOPF PHLC_CLOPF]] 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, causing cell rupture. 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.
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{{ABSTRACT_PUBMED_12009886}}
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==About this Structure==
==About this Structure==
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1KHO is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KHO OCA].
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[[1kho]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KHO OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:12009886</ref><references group="xtra"/>
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<ref group="xtra">PMID:012009886</ref><references group="xtra"/><references/>
[[Category: Clostridium perfringens]]
[[Category: Clostridium perfringens]]
[[Category: Basak, A K.]]
[[Category: Basak, A K.]]
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[[Category: C-terminal beta-sheet]]
[[Category: C-terminal beta-sheet]]
[[Category: N-terminal alpha-helix]]
[[Category: N-terminal alpha-helix]]
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[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:27:28 2009''
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Revision as of 10:34, 16 April 2014

Template:STRUCTURE 1kho

Contents

Crystal Structure Analysis of Clostridium perfringens alpha-Toxin Isolated from Avian Strain SWCP

Template:ABSTRACT PUBMED 12009886

Function

[PHLC_CLOPF] 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, causing cell rupture. 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.

About this Structure

1kho is a 2 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA.

Reference

  • Justin N, Walker N, Bullifent HL, Songer G, Bueschel DM, Jost H, Naylor C, Miller J, Moss DS, Titball RW, Basak AK. The first strain of Clostridium perfringens isolated from an avian source has an alpha-toxin with divergent structural and kinetic properties. Biochemistry. 2002 May 21;41(20):6253-62. PMID:12009886

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