1ah7: Difference between revisions
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==Overview== | ==Overview== | ||
Both the phosphatidylinositol-hydrolysing and the | 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 class and contains, at least in the crystalline state, three Zn2+ in the active site. We also present preliminary results from a study at 1.9 A resolution of the complex between PLC and inorganic phosphate (Pi) which indicate that the substrate binds directly to the metal ions. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: phospholipid hydrolysis]] | [[Category: phospholipid hydrolysis]] | ||
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Revision as of 12:44, 21 February 2008
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PHOSPHOLIPASE C FROM BACILLUS CEREUS
OverviewOverview
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 class and contains, at least in the crystalline state, three Zn2+ in the active site. We also present preliminary results from a study at 1.9 A resolution of the complex between PLC and inorganic phosphate (Pi) which indicate that the substrate binds directly to the metal ions.
About this StructureAbout this Structure
1AH7 is a Single protein structure of sequence from Bacillus cereus with as ligand. Active as Phospholipase C, with EC number 3.1.4.3 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
ReferenceReference
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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