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| Alpha toxin of Clostridium | ||
| Zinc dependent phospholipase C | ||
|---|---|---|
| Identifiers | ||
| Symbol | Zn_dep_PLPC | |
| Pfam | PF00882 | |
| InterPro | IPR001531 | |
| PROSITE | PDOC00357 | |
| SCOP | 1ah7 | |
| OPM family | 88 | |
| OPM protein | 1olp | |
| Available PDB structures:
1khoA:29-278 1olpB:29-278 1p5xA:39-282 1p6dA:39-282 1ah7 :39-282 1p6eA:39-282 |
||
Zinc dependent prokaryotic phospholipases C is a family of bacterial phospholipases C, some of which are also known as alpha toxins.
Bacillus cereus contains a monomeric phospholipase C EC 3.1.4.3 (PLC) of 245 amino-acid residues. Although PLC prefers to acton phosphatidylcholine, it also shows weak catalytic activity with sphingomyelin and phosphatidylinositol1. Sequence studies have shown the protein to be similar both to alpha toxin fromClostridium perfringens and Clostridium bifermentans, a phospholipase C involved in haemolysis and cell rupture2, and to lecithinase from Listeria monocytogenes, which aids cell-to-cell spread by breaking down the 2-membrane vacuoles that surround the bacterium during transfer3.
Each of these proteins is a zinc-dependent enzyme, binding 3 zinc ions per molecule4. The enzymes catalyse the conversion of phosphatidylcholine and water to 1,2-diacylglycerol and choline phosphate124.
In Bacillus cereus, there are nine residues known to be involved in binding the zinc ions: 5 His, 2 Asp, 1 Glu and 1 Trp. These residues are all conserved in the Clostridium alpha-toxin.
References
- ^ a b Nakamura S, Yamada A, Tsukagoshi N, Udaka S, Sasaki T, Makino S, Little C, Tomita M, Ikezawa H (1988). "Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus". Eur. J. Biochem. 175 (2): 213–220. doi:. PMID 2841128.
- ^ a b Titball RW, Rubidge T, Hunter SE, Martin KL, Morris BC, Shuttleworth AD, Anderson DW, Kelly DC (1989). "Molecular cloning and nucleotide sequence of the alpha-toxin (phospholipase C) of Clostridium perfringens". Infect. Immun. 57 (2): 367–376. PMID 2536355.
- ^ Kocks C, Dramsi S, Ohayon H, Geoffroy C, Mengaud J, Cossart P, Vazquez-Boland JA (1992). "Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread". Infect. Immun. 60 (1): 219–230. PMID 1309513.
- ^ a b Titball RW, Rubidge T (1990). "The role of histidine residues in the alpha toxin of Clostridium perfringens". FEMS Microbiol. Lett. 56 (3): 261–265. doi:. PMID 2111259.
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This article includes text from the public domain Pfam and InterPro IPR001531
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- This page was last modified on 26 November 2008, at 16:53.
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