1gyg
From Proteopedia
| Line 25: | Line 25: | ||
[[Category: zinc phospholipase c]] | [[Category: zinc phospholipase c]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:22:55 2007'' |
Revision as of 13:18, 30 October 2007
|
R32 CLOSED FORM OF ALPHA-TOXIN FROM CLOSTRIDIUM PERFRINGENS STRAIN CER89L43
Overview
Clostridium perfringens biotype A strains are the causative agents of, gas-gangrene in man and are also implicated as etiological agents in, sudden death syndrome in young domestic livestock. The main virulence, factor produced by these strains is a zinc-dependent, phosphatidylcholine-preferring phospholipase C (alpha-toxin). The crystal, structure of alpha-toxin, at pH 7.5, with the active site open and, therefore accessible to substrate has previously been reported, as has, calcium-binding to the C-terminal domain of the enzyme at pH 4.7. Here we, focus on conformation changes in the N-terminal domain of alpha-toxin in, crystals grown at acidic pH. These changes result in both the obscuring of, the toxin active site and the loss of one of three zinc ions from it., Additionally, this ... [(full description)]
About this Structure
1GYG 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 Site: ZA1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the C. perfringens alpha-toxin with the active site closed by a flexible loop region., Eaton JT, Naylor CE, Howells AM, Moss DS, Titball RW, Basak AK, J Mol Biol. 2002 May 31;319(2):275-81. PMID:12051905
Page seeded by OCA on Tue Oct 30 15:22:55 2007
