1AH7
PHOSPHOLIPASE C FROM BACILLUS CEREUS
Summary for 1AH7
| Entry DOI | 10.2210/pdb1ah7/pdb |
| Descriptor | PHOSPHOLIPASE C, ZINC ION (3 entities in total) |
| Functional Keywords | lipase, phospholipid hydrolysis, hydrolase |
| Biological source | Bacillus cereus |
| Total number of polymer chains | 1 |
| Total formula weight | 28619.65 |
| Authors | Greaves, R. (deposition date: 1997-04-14, release date: 1997-12-10, Last modification date: 2024-02-07) |
| Primary citation | Hough, E.,Hansen, L.K.,Birknes, B.,Jynge, K.,Hansen, S.,Hordvik, A.,Little, C.,Dodson, E.,Derewenda, Z. High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus. Nature, 338:357-360, 1989 Cited by PubMed Abstract: 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. PubMed: 2493587DOI: 10.1038/338357a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.501 Å) |
Structure validation
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