1qm6: Difference between revisions
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Revision as of 16:57, 30 October 2007
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R32 FORM OF CLOSTRIDIUM PERFRINGENS ALPHA-TOXIN STRAIN
OverviewOverview
Alpha-toxin is the key determinant in gas-gangrene. The toxin, a, phospholipase C, cleaves phosphatidylcholine in eukaryotic cell membranes., Calcium ions have been shown to be required for the specific binding of, toxin to membranes prior to phospholipid cleavage. Reported X-ray, crystallographic structures of the toxin show that the C-terminal domain, has a fold that is analogous to the eukaryotic calcium and, membrane-binding C2 domains. We report the binding sites for three calcium, ions that have been identified, by crystallographic methods, in the, C-terminal domain of the protein close to the postulated membrane-binding, surface. The position of these ions at the tip of the domain, and their, function (to facilitate membrane binding) is similar to that of calcium, ions observed ... [(full description)]
About this StructureAbout this Structure
1QM6 is a [Single protein] structure of sequence from [Clostridium perfringens] with ZN as [ligand]. Active as [Phospholipase C], with EC number [3.1.4.3]. Structure known Active Sites: ZN1, ZN2, ZN3 and ZN4. Full crystallographic information is available from [OCA].
ReferenceReference
Characterisation of the calcium-binding C-terminal domain of Clostridium perfringens alpha-toxin., Naylor CE, Jepson M, Crane DT, Titball RW, Miller J, Basak AK, Bolgiano B, J Mol Biol. 1999 Dec 3;294(3):757-70. PMID:10610794
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