Summary for 3X0D
| Entry DOI | 10.2210/pdb3x0d/pdb |
| Descriptor | Protein arginine N-methyltransferase 7, S-ADENOSYL-L-HOMOCYSTEINE, ZINC ION, ... (4 entities in total) |
| Functional Keywords | rossmann fold, transferase |
| Biological source | Caenorhabditis elegans (roundworm) |
| Total number of polymer chains | 1 |
| Total formula weight | 74544.75 |
| Authors | Hasegawa, M.,Toma-Fukai, S.,Shimizu, T. (deposition date: 2014-10-10, release date: 2014-10-29, 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 Cited by 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: 24726727DOI: 10.1016/j.febslet.2014.03.053 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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