Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Life Science Center, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8577, Japan.
FEBS Lett. 2014 May 21;588(10):1942-8. doi: 10.1016/j.febslet.2014.03.053. Epub 2014 Apr 12.
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.
精氨酸甲基转移酶 7（PRMT7）是一种能够催化 S-腺苷甲硫氨酸的甲基转移到精氨酸残基上的氮原子的酶家族成员。在这里，我们描述了秀丽隐杆线虫 PRMT7 与其反应产物 S-腺苷-L-同型半胱氨酸复合物的晶体结构。结构数据表明，PRMT7 含有两个串联重复的 PRMT 核心结构域，形成了一种新的同源二聚体样结构。S-腺苷-L-同型半胱氨酸仅结合到 N 端催化位点；C 端催化位点被一个抑制辅因子结合的环占据。突变分析表明，只有 PRMT7 的 N 端催化位点负责结合辅因子。
