9E3B
Cryo-EM structure of PRMT5/WDR77 in complex with 6S complex
Summary for 9E3B
| Entry DOI | 10.2210/pdb9e3b/pdb |
| EMDB information | 47476 47477 47478 |
| Descriptor | Protein arginine N-methyltransferase 5, Methylosome protein WDR77, Methylosome subunit pICln, ... (5 entities in total) |
| Functional Keywords | prmt5, methyl transferase, wdr77, arginine, transferase |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 16 |
| Total formula weight | 603366.15 |
| Authors | |
| Primary citation | Jin, C.Y.,Hunkeler, M.,Mulvaney, K.M.,Sellers, W.R.,Fischer, E.S. Substrate adaptors are flexible tethering modules that enhance substrate methylation by the arginine methyltransferase PRMT5. J.Biol.Chem., 301:108165-108165, 2025 Cited by PubMed Abstract: Protein arginine methyltransferase (PRMT) 5 is an essential arginine methyltransferase responsible for the majority of cellular symmetric dimethyl-arginine marks. PRMT5 uses substrate adaptors such as pICln, RIOK1, and COPR5 to recruit and methylate a wide range of substrates. Although the substrate adaptors play important roles in substrate recognition, how they direct PRMT5 activity towards specific substrates remains incompletely understood. Using biochemistry and cryogenic electron microscopy, we show that these adaptors compete for the same binding site on PRMT5. We find that substrate adaptor and substrate complexes are bound to PRMT5 through two peptide motifs, enabling these adaptors to act as flexible tethering modules to enhance substrate methylation. Taken together, our results shed structural and mechanistic light on the PRMT5 substrate adaptor function and the biochemical nature of PRMT5 interactors. PubMed: 39793893DOI: 10.1016/j.jbc.2025.108165 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.06 Å) |
Structure validation
Download full validation report
