1ORH

Structure of the Predominant Protein Arginine Methyltransferase PRMT1

1ORH の概要

• エントリーDOI: 10.2210/pdb1orh/pdb
• 関連するPDBエントリー: 1F3L 1OR8
• 分子名称: Protein arginine N-methyltransferase 1, Substrate peptide, S-ADENOSYL-L-HOMOCYSTEINE, ... (5 entities in total)
• 機能のキーワード: protein arginine methylation adomet-dependent methylation, transferase
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Nucleus (By similarity): Q63009
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41917.83

構造登録者

Zhang, X.,Cheng, X. (登録日: 2003-03-13, 公開日: 2003-08-26, 最終更新日: 2023-08-16)

主引用文献

Zhang, X.,Cheng, X.
Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of Its Binding to Substrate Peptides
Structure, 11:509-520, 2003

PubMed Abstract: PRMT1 is the predominant type I protein arginine methyltransferase in mammals and highly conserved among all eukaryotes. It is essential for early postimplantation development in mouse. Here we describe the crystal structure of rat PRMT1 in complex with the reaction product AdoHcy and a 19 residue substrate peptide containing three arginines. The results reveal a two-domain structure-an AdoMet binding domain and a barrel-like domain-with the active site pocket located between the two domains. Mutagenesis studies confirmed that two active site glutamates are essential for enzymatic activity, and that dimerization of PRMT1 is essential for AdoMet binding. Three peptide binding channels are identified: two are between the two domains, and the third is on the surface perpendicular to the strands forming the beta barrel.

PubMed: 12737817
DOI: 10.1016/S0969-2126(03)00071-6

実験手法

X-RAY DIFFRACTION (2.64 Å)