5dst | pdb_00005dst
Crystal structure of human PRMT8 in complex with SAH
Structural highlights
FunctionANM8_HUMAN Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS.[1] [2] [3] Publication Abstract from PubMedProtein 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 3.0A 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. Novel helical assembly in arginine methyltransferase 8.,Toma-Fukai S, Kim JD, Park KE, Kuwabara N, Shimizu N, Krayukuhina E, Uchiyama S, Fukamizu A, Shimizu T J Mol Biol. 2016 Feb 11. pii: S0022-2836(16)00112-1. doi:, 10.1016/j.jmb.2016.02.007. PMID:26876602[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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