3F9Q

Re-refinement of uncomplexed plasmepsin II from Plasmodium falciparum.

3F9Q の概要

• エントリーDOI: 10.2210/pdb3f9q/pdb
• 関連するPDBエントリー: 1LF4
• 分子名称: Plasmepsin-2 (2 entities in total)
• 機能のキーワード: hydrolase, aspartyl protease, glycoprotein, protease, vacuole, zymogen
• 由来する生物種: Plasmodium falciparum
• 細胞内の位置: Vacuole: P46925
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36909.62

構造登録者

Robbins, A.H.,Mckenna, R. (登録日: 2008-11-14, 公開日: 2009-03-10, 最終更新日: 2024-10-16)

主引用文献

Robbins, A.H.,Dunn, B.M.,Agbandje-McKenna, M.,McKenna, R.
Crystallographic evidence for noncoplanar catalytic aspartic acids in plasmepsin II resides in the Protein Data Bank.
Acta Crystallogr.,Sect.D, 65:294-296, 2009

PubMed Abstract: The carboxylate atoms of the two catalytic aspartic acid residues in aspartic proteases are nearly coplanar and in the uncomplexed form share an in-plane nucleophilic water molecule that is central to the mechanism of these enzymes. This note reports that while reviewing the electron-density maps derived from the deposited data for uncomplexed plasmepsin II from Plasmodium falciparum [Asojo et al. (2003), J. Mol. Biol. 327, 173-181; PDB code 1lf4], it was discovered that the aspartic acid residues in this structure should in fact be distinctly noncoplanar. The crystallographic model from the deposited coordinates has been re-refined against the 1.9 A resolution published diffraction data to an R(cryst) of 21.2% and an R(free) of 22.2%. The catalytic water molecule is present, but the plane of the carboxylate group of Asp214 is rotated by 66 degrees from its original position.

PubMed: 19237752
DOI: 10.1107/S0907444908041632

実験手法

X-RAY DIFFRACTION (1.9 Å)