1PTG

PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C IN COMPLEX WITH MYO-INOSITOL

1PTG の概要

• エントリーDOI: 10.2210/pdb1ptg/pdb
• 分子名称: PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C, 1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE (3 entities in total)
• 機能のキーワード: hydrolase, phosphatidylinositol specific phospholipase c, myo-inositol, inhibitor complex, hydrolase (phosphoric diester)
• 由来する生物種: Bacillus cereus
• 細胞内の位置: Secreted: P14262
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34748.82

構造登録者

Heinz, D.W.,Ryan, M.,Bullock, T.L.,Griffith, O.H. (登録日: 1995-05-24, 公開日: 1996-07-11, 最終更新日: 2024-02-14)

主引用文献

Heinz, D.W.,Ryan, M.,Bullock, T.L.,Griffith, O.H.
Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol.
EMBO J., 14:3855-3863, 1995

PubMed Abstract: Phosphatidylinositol (PI), once regarded as an obscure component of membranes, is now recognized as an important reservoir of second messenger precursors and as an anchor for membrane enzymes. PI-specific phospholipase C (PI-PLC) is the enzyme that cleaves PI, invoking numerous cellular responses. The crystal structure of PI-PLC from Bacillus cereus (EC 3.1.4.10) has been solved at 2.6 A resolution and refined to a crystallographic R factor of 18.7%. The structure consists of an imperfect (beta alpha)8-barrel similar to that first observed for triose phosphate isomerase and does not resemble any other known phospholipase structure. The active site of the enzyme has been identified by determining the structure of PI-PLC in complex with its inhibitor, myo-inositol, at 2.6 A resolution (R factor = 19.5%). This substrate-like inhibitor interacts with a number of residues highly conserved among prokaryotic PI-PLCs. Residues His32 and His82, which are also conserved between prokaryotic and eukaryotic PI-PLCs, most likely act as general base and acid respectively in a catalytic mechanism analogous to that observed for ribonucleases.

PubMed: 7664726

実験手法

X-RAY DIFFRACTION (2.6 Å)