3WST

Crystal structure of C.elegans PRMT7 in complex with SAH(P31)

Summary for 3WST

• Entry DOI: 10.2210/pdb3wst/pdb
• Descriptor: Protein arginine N-methyltransferase 7, S-ADENOSYL-L-HOMOCYSTEINE, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: rossmann fold, transferase
• Biological source: Caenorhabditis elegans (roundworm)
• Total number of polymer chains: 18
• Total formula weight: 1342337.62

Authors

Hasegawa, M.,Toma-fukai, S.,Shimizu, T. (deposition date: 2014-03-21, release date: 2014-04-23, Last modification date: 2024-03-20)

Primary citation

Hasegawa, M.,Toma-fukai, S.,Kim, J.D.,Fukamizu, A.,Shimizu, T.
Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats
Febs Lett., 588:1942-1948, 2014

PubMed 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.

PubMed: 24726727
DOI: 10.1016/j.febslet.2014.03.053

Experimental method

X-RAY DIFFRACTION (2.39 Å)