2DE9

Crystal structure of porcine pancreatic elastase complexed with Tris after soaking a tris-free solution

2DE9 の概要

• エントリーDOI: 10.2210/pdb2de9/pdb
• 関連するPDBエントリー: 2DE8
• 分子名称: Elastase-1, SULFATE ION (3 entities in total)
• 機能のキーワード: serine protease, hydrolase
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P00772
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26121.14

構造登録者

Kinoshita, T.,Tada, T. (登録日: 2006-02-09, 公開日: 2006-07-11, 最終更新日: 2024-10-23)

主引用文献

Kinoshita, T.,Yamaguchi, A.,Tada, T.
Tris(hydroxymethyl)aminomethane induces conformational change and crystal-packing contraction of porcine pancreatic elastase.
Acta Crystallogr.,Sect.F, 62:623-626, 2006

PubMed Abstract: Porcine pancreatic elastase (PPE) was crystallized under new sulfate-free conditions containing 0.3 M NaCl and 50 mM tris(hydroxymethyl)aminomethane-HCl at pH 7.0. The crystal structure determined at 1.5 angstroms resolution had a unique conformation in four regions which contained loop portions. A chloride ion was bound near the catalytic triad instead of the sulfate ion in PDB entry 1qnj, a typical PPE crystal structure. However, the chloride ion did not affect the configuration of the catalytic triad. A tris(hydroxymethyl)aminomethane (Tris) molecule was bound to the S4 and S5 subsites in place of the adjacent molecule in the 1qnj crystal and played a significant role in the structural change of the region. The distortion in this region may subsequently have induced conformational changes in the other three regions. The fact that Tris and these four regions make a diagonal line in the ac plane may have affected the crystal-packing contraction along the a and c axes in the crystal compared with the typical crystal.

PubMed: 16820677
DOI: 10.1107/S1744309106023001

実験手法

X-RAY DIFFRACTION (1.3 Å)