1PIR

SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2

1PIR の概要

• エントリーDOI: 10.2210/pdb1pir/pdb
• 分子名称: PHOSPHOLIPASE A2, CALCIUM ION (2 entities in total)
• 機能のキーワード: phospholipase a2, phosphatide-2-acyl-hydrolase, pla2, carboxylic ester hydrolase
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P00592
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14049.79

構造登録者

Van Den Berg, B.D.,Tessari, M.,De Haas, G.H.,Verheij, H.M.,Boelens, R.,Kaptein, R. (登録日: 1994-12-22, 公開日: 1995-06-03, 最終更新日: 2024-11-20)

主引用文献

van den Berg, B.,Tessari, M.,de Haas, G.H.,Verheij, H.M.,Boelens, R.,Kaptein, R.
Solution structure of porcine pancreatic phospholipase A2.
EMBO J., 14:4123-4131, 1995

PubMed Abstract: The lipolytic enzyme phospholipase A2 (PLA2) is involved in the degradation of high-molecular weight phospholipid aggregates in vivo. The enzyme has very high catalytic activities on aggregated substrates compared with monomeric substrates, a phenomenon called interfacial activation. Crystal structures of PLA2s in the absence and presence of inhibitors are identical, from which it has been concluded that enzymatic conformational changes do not play a role in the mechanism of interfacial activation. The high-resolution NMR structure of porcine pancreatic PLA2 free in solution was determined with heteronuclear multidimensional NMR methodology using doubly labeled 13C, 15N-labeled protein. The solution structure of PLA2 shows important deviations from the crystal structure. In the NMR structure the Ala1 alpha-amino group is disordered and the hydrogen bonding network involving the N-terminus and the active site is incomplete. The disorder observed for the N-terminal region of PLA2 in the solution structure could be related to the low activity of the enzyme towards monomeric substrates. The NMR structure of PLA2 suggests, in contrast to the crystallographic work, that conformational changes do play a role in the interfacial activation of this enzyme.

PubMed: 7556053

実験手法

SOLUTION NMR