1ah7
From Proteopedia
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[[Category: phospholipid hydrolysis]] | [[Category: phospholipid hydrolysis]] | ||
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Revision as of 12:43, 30 October 2007
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PHOSPHOLIPASE C FROM BACILLUS CEREUS
Overview
Both the phosphatidylinositol-hydrolysing and the, phosphatidylcholine-hydrolysing phospholipases C have been implicated in, the generation of second messengers in mammalian cells. The, phosphatidylcholine-hydrolysing phospholipase C (PLC) from Bacillus, cereus, a monomeric protein containing 245 amino-acid residues, is similar, to some of the corresponding mammalian proteins. This, together with the, fact that the bacterial enzyme can mimic the action of mammalian PLC in, causing, for example, enhanced prostaglandin biosynthesis, suggests that, B. cereus PLC can be used as a model for the hitherto poorly characterized, mammalian PLCs. We report here the three-dimensional structure of B., cereus PLC at 1.5 A resolution. The enzyme is an all-helix protein, belonging to a novel structural ... [(full description)]
About this Structure
1AH7 is a [Single protein] structure of sequence from [Bacillus cereus] with ZN as [ligand]. Active as [Phospholipase C], with EC number [3.1.4.3]. Structure known Active Sites: CAT, ZNA, ZNB and ZNC. Full crystallographic information is available from [OCA].
Reference
High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus., Hough E, Hansen LK, Birknes B, Jynge K, Hansen S, Hordvik A, Little C, Dodson E, Derewenda Z, Nature. 1989 Mar 23;338(6213):357-60. PMID:2493587
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