1ah7: Difference between revisions
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==Overview== | ==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 .. | 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== | ||
1AH7 is a | 1AH7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] Structure known Active Sites: CAT, ZNA, ZNB and ZNC. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AH7 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: phospholipid hydrolysis]] | [[Category: phospholipid hydrolysis]] | ||
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Revision as of 14:59, 5 November 2007
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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 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.
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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