2PLL

Crystal structure of perdeuterated human arginase I

2PLL の概要

• エントリーDOI: 10.2210/pdb2pll/pdb
• 関連するPDBエントリー: 2AEB
• 分子名称: arginase-1, MANGANESE (II) ION, 2(S)-AMINO-6-BORONOHEXANOIC ACID, ... (4 entities in total)
• 機能のキーワード: perdeuterated protein; x-ray structure, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P05089
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70163.51

構造登録者

Di Costanzo, L.,Moulin, M.,Haertlein, M.,Meilleur, F.,Christianson, D.W. (登録日: 2007-04-19, 公開日: 2007-08-14, 最終更新日: 2023-08-30)

主引用文献

Di Costanzo, L.,Moulin, M.,Haertlein, M.,Meilleur, F.,Christianson, D.W.
Expression, purification, assay, and crystal structure of perdeuterated human arginase I
Arch.Biochem.Biophys., 465:82-89, 2007

PubMed Abstract: Arginase is a manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to yield l-ornithine and urea. In order to establish a foundation for future neutron diffraction studies that will provide conclusive structural information regarding proton/deuteron positions in enzyme-inhibitor complexes, we have expressed, purified, assayed, and determined the X-ray crystal structure of perdeuterated (i.e., fully deuterated) human arginase I complexed with 2(S)-amino-6-boronohexanoic acid (ABH) at 1.90A resolution. Prior to the neutron diffraction experiment, it is important to establish that perdeuteration does not cause any unanticipated structural or functional changes. Accordingly, we find that perdeuterated human arginase I exhibits catalytic activity essentially identical to that of the unlabeled enzyme. Additionally, the structure of the perdeuterated human arginase I-ABH complex is identical to that of the corresponding complex with the unlabeled enzyme. Therefore, we conclude that crystals of the perdeuterated human arginase I-ABH complex are suitable for neutron crystallographic study.

PubMed: 17562323
DOI: 10.1016/j.abb.2007.04.036

実験手法

X-RAY DIFFRACTION (1.9 Å)