Journal
FEBS LETTERS
Volume 588, Issue 10, Pages 1942-1948Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2014.03.053
Keywords
Protein arginine methyltransferase; S-adenosyl-L-homocysteine; X-ray crystallography
Funding
- Japanese Ministry of Education, Culture, Sports, Science, and Technology
- Takeda Science Foundation
- Grants-in-Aid for Scientific Research [25252062] Funding Source: KAKEN
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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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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