2ZP4

Carboxylic ester hydrolase, single mutant h48n of bovine pancreatic pla2 enzyme

2ZP4 の概要

• エントリーDOI: 10.2210/pdb2zp4/pdb
• 関連するPDBエントリー: 2ZP3 2ZP5
• 分子名称: Phospholipase A2, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, active site mutant, metal binding protein, calcium, lipid degradation, metal-binding, pyrrolidone carboxylic acid, secreted
• 由来する生物種: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• 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: 14020.24

構造登録者

Kanaujia, S.P.,Sekar, K. (登録日: 2008-06-27, 公開日: 2008-11-04, 最終更新日: 2024-10-30)

主引用文献

Kanaujia, S.P.,Sekar, K.
Structures and molecular-dynamics studies of three active-site mutants of bovine pancreatic phospholipase A(2)
Acta Crystallogr.,Sect.D, 64:1003-1011, 2008

PubMed Abstract: Phospholipase A(2) hydrolyzes phospholipids at the sn-2 position to cleave the fatty-acid ester bond of L-glycerophospholipids. The catalytic dyad (Asp99 and His48) along with a nucleophilic water molecule is responsible for enzyme hydrolysis. Furthermore, the residue Asp49 in the calcium-binding loop is essential for controlling the binding of the calcium ion and the catalytic action of phospholipase A(2). To elucidate the structural role of His48 and Asp49, the crystal structures of three active-site single mutants H48N, D49N and D49K have been determined at 1.9 A resolution. Although the catalytically important calcium ion is present in the H48N mutant, the crystal structure shows that proton transfer is not possible from the catalytic water to the mutated residue. In the case of the Asp49 mutants, no calcium ion was found in the active site. However, the tertiary structures of the three active-site mutants are similar to that of the trigonal recombinant enzyme. Molecular-dynamics simulation studies provide a good explanation for the crystallographic results.

PubMed: 18931407
DOI: 10.1107/S0907444908022713

実験手法

X-RAY DIFFRACTION (1.9 Å)