5DST
Crystal structure of human PRMT8 in complex with SAH
Summary for 5DST
| Entry DOI | 10.2210/pdb5dst/pdb |
| Descriptor | Protein arginine N-methyltransferase 8, S-ADENOSYL-L-HOMOCYSTEINE (2 entities in total) |
| Functional Keywords | methyltransferase, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 15 |
| Total formula weight | 583447.57 |
| Authors | Toma-Fukai, S.,Shimizu, T. (deposition date: 2015-09-17, release date: 2016-02-24, Last modification date: 2024-03-20) |
| Primary citation | Toma-Fukai, S.,Kim, J.D.,Park, K.E.,Kuwabara, N.,Shimizu, N.,Krayukhina, E.,Uchiyama, S.,Fukamizu, A.,Shimizu, T. Novel helical assembly in arginine methyltransferase 8 J.Mol.Biol., 428:1197-1208, 2016 Cited by PubMed Abstract: Protein arginine methyltransferase 8 (PRMT8) is unique among PRMTs, as it is specifically expressed in brain and localized to the plasma membrane via N-terminal myristoylation. Here, we describe the crystal structure of human PRMT8 (hPRMT8) at 3.0-Å resolution. The crystal structure of hPRMT8 exhibited a novel helical assembly. Biochemical, biophysical and mutagenesis experiments demonstrated that hPRMT8 forms an octamer in solution. This octameric structure is necessary for proper localization to the plasma membrane and efficient methyltransferase activity. The helical assembly might be a relevant quaternary form for hPRMT1, which is the predominant PRMT in mammalian cells and most closely related to hPRMT8. PubMed: 26876602DOI: 10.1016/j.jmb.2016.02.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.963 Å) |
Structure validation
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