6JUZ

Crystal Structure of N-terminal domain of ArgZ(N71S) covalently bond to a reaction intermediate

6JUZ の概要

• エントリーDOI: 10.2210/pdb6juz/pdb
• 分子名称: Sll1336 protein, ARGININE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: arginine dihydrolase, amidino-transferase domain, alpha/beta propeller fold, (lor/sdh superfamily), hydrolase
• 由来する生物種: Synechocystis sp. (strain PCC 6803 / Kazusa)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35345.30

構造登録者

Zhuang, N.,Li, L.,Wu, X.,Zhuang, Y. (登録日: 2019-04-15, 公開日: 2020-01-15, 最終更新日: 2023-11-22)

主引用文献

Zhuang, N.,Zhang, H.,Li, L.,Wu, X.,Yang, C.,Zhang, Y.
Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond rotation" catalytic mechanism.
J.Biol.Chem., 295:2113-2124, 2020

PubMed Abstract: A recently discovered ornithine-ammonia cycle (OAC) serves as a conduit in the nitrogen storage and remobilization machinery in cyanobacteria. The OAC involves an arginine catabolic reaction catalyzed by the arginine dihydrolase ArgZ whose catalytic mechanism is unknown. Here we determined the crystal structures at 1.2-3.0 Å of unliganded ArgZ from the cyanobacterium sp. PCC6803 and of ArgZ complexed with its substrate arginine, a covalently linked reaction intermediate, or the reaction product ornithine. The structures reveal that a key residue, Asn, in the ArgZ active center functions as the determinant distinguishing ArgZ from other members of the guanidino group-modifying enzyme superfamily. The structures, along with biochemical evidence from enzymatic assays coupled with electrospray ionization MS techniques, further suggest that ArgZ-catalyzed conversion of arginine to ornithine, ammonia, and carbon dioxide consists of two successive cycles of amine hydrolysis. Finally, we show that arginine dihydrolases are broadly distributed among bacteria and metazoans, suggesting that the OAC may be frequently used for redistribution of nitrogen from arginine catabolism or nitrogen fixation.

PubMed: 31914412
DOI: 10.1074/jbc.RA119.011752

実験手法

X-RAY DIFFRACTION (1.21 Å)