Protein arginine methyltransferase 7 has a novel homodimer‐like structure formed by tandem repeats. Issue 10 (12th April 2014)

• Record Type: Journal Article
• Authors: Hasegawa, Morio; Toma-Fukai, Sachiko; Kim, Jun-Dal; Fukamizu, Akiyoshi; Shimizu, Toshiyuki
• Is Part Of: FEBS letters. Volume 588:Issue 10(2014)
• Page Start: 1942
• Page End: 1948
• Publication Date: 2014-04-12
• Subjects: AdoMet -- S-adenosyl-l-methionine -- AdoHcy -- S-adenosyl-l-homocysteine -- SAXS -- small-angle X-ray scattering -- Protein arginine methyltransferase -- S-adenosyl-l-homocysteine -- X-ray crystallography; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2014.03.053
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract : CePRMT7 is a member of PRMT7 subfamily and harbors two tandem repeated PRMT core domains. The crystal structure of PRMT7 in complex with SAH was determined. A single PRMT7 molecule forms a homodimer‐like arrangement. The structural features strongly suggest that PRMT7 functions as a type III enzyme.