2B96

Third Calcium ion found in an inhibitor bound phospholipase A2

2B96 の概要

• エントリーDOI: 10.2210/pdb2b96/pdb
• 関連するPDBエントリー: 1mkt 1une
• 分子名称: Phospholipase A2, CALCIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: alpha helix, beta sheet, triple mutant, anisic acid, hydrolase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted: P00593
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14612.96

構造登録者

Sekar, K.,Velmurugan, D.,Yamane, T.,Tsai, M.D. (登録日: 2005-10-11, 公開日: 2006-03-28, 最終更新日: 2024-10-30)

主引用文献

Sekar, K.,Gayathri, D.,Velmurugan, D.,Jeyakanthan, J.,Yamane, T.,Poi, M.J.,Tsai, M.D.
Third Calcium ion found in an inhibitor bound phospholipase A2
Acta Crystallogr.,Sect.D, 62:392-397, 2006

PubMed Abstract: The lipolytic enzyme phospholipase A2 plays a crucial role in lipid metabolism and catalyzes hydrolysis of the fatty-acid ester bond at the sn-2 position of phospholipids. Here, the crystal structure (1.7 A resolution) of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 complexed with an organic molecule, p-methoxybenzoic acid (anisic acid), is reported. Residues 60-70 (the surface-loop residues) are ordered and adopt conformations which are different from those normally found in structures in which a second calcium ion is present. It is interesting to note that for the first time a third calcium ion has been identified. In addition, four Tris (2-amino-2-hydroxymethyl-1,3-propanediol) molecules were located. It is believed that one of the Tris molecules plays a role in clamping the third calcium ion and that another is involved in controlling the dynamics of the surface loop through hydrogen bonds.

PubMed: 16552140
DOI: 10.1107/S0907444906001612

実験手法

X-RAY DIFFRACTION (1.7 Å)