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Protein arginine methyltransferase 7 has a novel homodimer‐like structure formed by tandem repeats
Author(s) -
Hasegawa Morio,
Toma-Fukai Sachiko,
Kim Jun-Dal,
Fukamizu Akiyoshi,
Shimizu Toshiyuki
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.03.053
Subject(s) - methyltransferase , cofactor , chemistry , arginine , mutagenesis , catalytic cycle , biochemistry , binding site , stereochemistry , protein structure , enzyme , active site , transferase , methylation , mutation , amino acid , dna , gene
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.