21ZH
Cryo-EM structure of NSUN2-tRNAlys-SAM
Summary for 21ZH
| Entry DOI | 10.2210/pdb21zh/pdb |
| EMDB information | 68111 |
| Descriptor | NSUN2, tRNAlys (77-MER), S-ADENOSYLMETHIONINE (3 entities in total) |
| Functional Keywords | trna, m5c rna methyltransferase, nsun2, transferase/rna, transferase-rna complex |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 111718.79 |
| Authors | |
| Primary citation | Hu, Q.,Yang, W.,Yu, Y.,Yi, R.,Zhang, Y.,Duan, L.,Li, F.,Zhang, K.,Gong, Q.,Li, S. Structure-driven RNA remodeling underlies broad substrate recognition by NSUN2. Sci China Life Sci, 2026 Cited by PubMed Abstract: The human RNA mC methyltransferase NSUN2 catalyzes site-specific cytosine methylation across diverse RNA substrates and thereby regulates a wide range of biological and physiological processes. However, the molecular basis by which NSUN2 achieves broad substrate recognition while maintaining catalytic specificity has remained unclear. Here, we determine structures of human NSUN2 in both substrate-free and substrate-bound states using X-ray crystallography and cryo-electron microscopy. Structures of NSUN2 in complex with multiple tRNA substrates reveal a structure-first, sequence-tolerant strategy in which NSUN2 actively remodels tRNA architecture, exposing the buried target cytosine and positioning it within the catalytic pocket for methyl transfer. This recognition strategy enables NSUN2 to accommodate diverse tRNA substrates through a largely conserved interaction interface. Together, our findings define the molecular principles underlying NSUN2-mediated RNA mC modification. PubMed: 42258135DOI: 10.1007/s11427-026-3373-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
No wwPDB Validation report is currently available for this entry.
