2RD5

Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana

2RD5 の概要

• エントリーDOI: 10.2210/pdb2rd5/pdb
• 関連するPDBエントリー: 2O66 2O67
• 分子名称: Acetylglutamate kinase-like protein, PII protein, ARGININE, ... (8 entities in total)
• 機能のキーワード: protein-protein complex, regulation of arginine biosynthesis, nitrogen metabolism, kinase, transferase, transcription, transcription regulation, protein binding
• 由来する生物種: Arabidopsis thaliana (thale cress); 詳細
• 細胞内の位置: Plastid, chloroplast stroma : Q9SCL7; Plastid, chloroplast : Q9ZST4
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 94738.65

構造登録者

Mizuno, Y.,Moorhead, G.B.G.,Ng, K.K.S. (登録日: 2007-09-21, 公開日: 2007-10-02, 最終更新日: 2023-08-30)

主引用文献

Mizuno, Y.,Moorhead, G.B.,Ng, K.K.
Structural Basis for the Regulation of N-Acetylglutamate Kinase by PII in Arabidopsis thaliana.
J.Biol.Chem., 282:35733-35740, 2007

PubMed Abstract: PII is a highly conserved regulatory protein found in organisms across the three domains of life. In cyanobacteria and plants, PII relieves the feedback inhibition of the rate-limiting step in arginine biosynthesis catalyzed by N-acetylglutamate kinase (NAGK). To understand the molecular structural basis of enzyme regulation by PII, we have determined a 2.5-A resolution crystal structure of a complex formed between two homotrimers of PII and a single hexamer of NAGK from Arabidopsis thaliana bound to the metabolites N-acetylglutamate, ADP, ATP, and arginine. In PII, the T-loop and Trp(22) at the start of the alpha1-helix, which are both adjacent to the ATP-binding site of PII, contact two beta-strands as well as the ends of two central helices (alphaE and alphaG) in NAGK, the opposing ends of which form major portions of the ATP and N-acetylglutamate substrate-binding sites. The binding of Mg(2+).ATP to PII stabilizes a conformation of the T-loop that favors interactions with both open and closed conformations of NAGK. Interactions between PII and NAGK appear to limit the degree of opening and closing of the active-site cleft in opposition to a domain-separating inhibitory effect exerted by arginine, thus explaining the stimulatory effect of PII on the kinetics of arginine-inhibited NAGK.

PubMed: 17913711
DOI: 10.1074/jbc.M707127200

実験手法

X-RAY DIFFRACTION (2.51 Å)