1olp
From Proteopedia
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[[Category: zinc phospholipase c]] | [[Category: zinc phospholipase c]] | ||
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Revision as of 13:53, 30 October 2007
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ALPHA TOXIN FROM CLOSTRIDIUM ABSONUM
Overview
Clostridium absonum phospholipase C (Caa) is a 42.7 kDa protein, which, shows 60% amino acid sequence identity with the Clostridium perfringens, phospholipase C, or alpha-toxin (Cpa), and has been isolated from patients, suffering from gas gangrene. We report the cloning and sequencing, purification, characterisation and crystal structure of the Caa enzyme., Caa had twice the phospholipid-hydrolysing (lecithinase) activity, 1.5, times the haemolytic activity and over seven times the activity towards, phosphatidylcholine-based liposomes when compared with Cpa. However, the, Caa enzyme had a lower activity than Cpa to the free (i.e. not in lipid, bilayer) substrate para-nitrophenylphosphorylcholine, towards, sphingomyelin-based liposomes and showed half the cytotoxicity. The lethal, dose ... [(full description)]
About this Structure
1OLP is a [Single protein] structure of sequence from [Clostridium sardiniense] with CA and ZN as [ligands]. Active as [Phospholipase C], with EC number [3.1.4.3]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Clostridium absonum alpha-toxin: new insights into clostridial phospholipase C substrate binding and specificity., Clark GC, Briggs DC, Karasawa T, Wang X, Cole AR, Maegawa T, Jayasekera PN, Naylor CE, Miller J, Moss DS, Nakamura S, Basak AK, Titball RW, J Mol Biol. 2003 Oct 31;333(4):759-69. PMID:14568535
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