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Publication Abstract from PubMed

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.

Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats.,Hasegawa M, Toma-Fukai S, Kim JD, Fukamizu A, Shimizu T FEBS Lett. 2014 Apr 9. pii: S0014-5793(14)00272-5. doi:, 10.1016/j.febslet.2014.03.053. PMID:24726727^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.