3X0D

Crystal structure of C.elegans PRMT7 in complex with SAH (P43212)

「3WSS」から置き換えられました

3X0D の概要

• エントリーDOI: 10.2210/pdb3x0d/pdb
• 分子名称: Protein arginine N-methyltransferase 7, S-ADENOSYL-L-HOMOCYSTEINE, ZINC ION, ... (4 entities in total)
• 機能のキーワード: rossmann fold, transferase
• 由来する生物種: Caenorhabditis elegans (roundworm)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 74544.75

構造登録者

Hasegawa, M.,Toma-Fukai, S.,Shimizu, T. (登録日: 2014-10-10, 公開日: 2014-10-29, 最終更新日: 2024-03-20)

主引用文献

Hasegawa, M.,Toma-fukai, S.,Kim, J.D.,Fukamizu, A.,Shimizu, T.
Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats
Febs Lett., 588:1942-1948, 2014

PubMed Abstract: Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues. Here, we describe the crystal structure of Caenorhabditis elegans PRMT7 in complex with its reaction product S-adenosyl-L-homocysteine. The structural data indicated that PRMT7 harbors two tandem repeated PRMT core domains that form a novel homodimer-like structure. S-adenosyl-L-homocysteine bound to the N-terminal catalytic site only; the C-terminal catalytic site is occupied by a loop that inhibits cofactor binding. Mutagenesis demonstrated that only the N-terminal catalytic site of PRMT7 is responsible for cofactor binding.

PubMed: 24726727
DOI: 10.1016/j.febslet.2014.03.053

実験手法

X-RAY DIFFRACTION (2.15 Å)