1S9R

CRYSTAL STRUCTURE OF ARGININE DEIMINASE COVALENTLY LINKED WITH A REACTION INTERMEDIATE

1S9R の概要

• エントリーDOI: 10.2210/pdb1s9r/pdb
• 関連するPDBエントリー: 1LXY
• 分子名称: Arginine deiminase, ARGININE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• 機能のキーワード: deiminase, hydrolase, 5-fold pseudo-symmetric domain, 5-helix bundle domain, raction intermediate
• 由来する生物種: Mycoplasma arginini
• 細胞内の位置: Cytoplasm (Potential): P23793
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93721.06

構造登録者

Das, K.,Buttler, G.H.,Kwiatkowski, V.,Clark Jr., A.D.,Yadav, P.,Arnold, E. (登録日: 2004-02-05, 公開日: 2004-04-13, 最終更新日: 2024-10-30)

主引用文献

Das, K.,Buttler, G.H.,Kwiatkowski, V.,Clark Jr., A.D.,Yadav, P.,Arnold, E.
Crystal Structures of Arginine Deiminase with Covalent Reaction Intermediates: Implications for Catalytic Mechanism
Structure, 12:657-667, 2004

PubMed Abstract: Arginine deiminase (ADI), an enzyme that hydrolyzes arginine to generate energy in many parasitic microorganisms, has potent anticancer activities and can halt growth of solid tumors. We determined the crystal structure of ADI from Mycoplasma arginini in two different forms (1.6 and 2.0 A resolution) using multiple isomorphous replacement. ADI shares common structural features with the arginine-catabolizing enzymes Arg:Gly amidinotransferase and dimethylarginine dimethyl-aminohydrolase; ADI contains an additional domain of five helices. The scissile C-N bonds of the substrates and the catalytic triads (Cys398-His269-Glu213 of ADI) for the three enzymes superimpose on each other. The ADI structure from form I crystals corresponds to a tetrahedral intermediate with four heteroatoms (1S, 2N, 1O) covalently bonded to the reaction-center carbon. The structure from form II crystals represents an amidino-enzyme complex; the reaction-center carbon is covalently bonded to Cys398 sulfur and two nitrogens, and the reacting water molecule is only 2.54 A away.

PubMed: 15062088
DOI: 10.1016/j.str.2004.02.017

実験手法

X-RAY DIFFRACTION (1.6 Å)