1AH7

PHOSPHOLIPASE C FROM BACILLUS CEREUS

1AH7 の概要

• エントリーDOI: 10.2210/pdb1ah7/pdb
• 分子名称: PHOSPHOLIPASE C, ZINC ION (3 entities in total)
• 機能のキーワード: lipase, phospholipid hydrolysis, hydrolase
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28619.65

構造登録者

Greaves, R. (登録日: 1997-04-14, 公開日: 1997-12-10, 最終更新日: 2024-02-07)

主引用文献

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

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: 2493587
DOI: 10.1038/338357a0

実験手法

X-RAY DIFFRACTION (1.501 Å)