Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Substrate selectivity of the human RNA mC methyltransferase NSUN2.
Journal, issue, pages	Nature, Year 2026
Publish date	May 27, 2026
Authors	Jacob Canepa / Victor M Ruiz-Arroyo / Netanya S Schlamowitz / Yunsun Nam /
PubMed Abstract	Specific deposition of RNA modifications is important for regulating gene expression. 5-Methylcytosine (mC) is a common epitranscriptomic modification, and NSUN2 is a key enzyme responsible for mC ...Specific deposition of RNA modifications is important for regulating gene expression. 5-Methylcytosine (mC) is a common epitranscriptomic modification, and NSUN2 is a key enzyme responsible for mC methylation of various types of RNA. Dysregulation of NSUN2 is associated with numerous diseases, including cancers and neurological disorders. The versatility of NSUN2 complicates our understanding of its substrate specificity and molecular roles in biology and disease. Here we show how NSUN2 interacts with RNA substrates at distinct stages of its catalytic cycle to modify cytidines. Furthermore, we show the role of RNA structure in facilitating NSUN2 activity at multiple tRNA positions. We identify RNA duplexes surrounding the mC modification site as crucial recognition elements for methylation, which enabled us to derive a minimized substrate that captures the preferred features of an NSUN2 substrate-a dual-stem structure containing the CNNRR motif at the 5' end of the first stem. Insights into the mechanisms underlying substrate-specific NSUN2 enzymatic activity provide opportunities for understanding and therapeutically targeting NSUN2-dependent methylation. Overall, our work highlights the roles of RNA structure and sequence in defining substrate specificity and regulating RNA-modifying enzymes.
External links	Nature / PubMed:42203868
Methods	EM (single particle)
Resolution	2.57 - 3.71 Å
Structure data	73772 9z2n EMDB-73772, PDB-9z2n: CryoEM structure of human NSUN2(C271A) with SAH cross-linked to tRNA Lys(CTT) (D-arm conformation) Method: EM (single particle) / Resolution: 2.57 Å 73773 9z2o EMDB-73773, PDB-9z2o: CryoEM structure of human NSUN2(C271A) with SAH cross-linked to tRNA Lys(CTT) (No D-arm conformation) Method: EM (single particle) / Resolution: 2.66 Å 73774 9z2p EMDB-73774, PDB-9z2p: CryoEM structure of human NSUN2 with tRNA Lys(CTT) (Conformation 1) Method: EM (single particle) / Resolution: 2.91 Å 73775 9z2q EMDB-73775, PDB-9z2q: CryoEM structure of human NSUN2 with tRNA Lys(CTT) (Conformation 2) Method: EM (single particle) / Resolution: 2.88 Å 73776 9z2r EMDB-73776, PDB-9z2r: CryoEM structure of human NSUN2 with tRNA Lys(CTT) and SFG (D-arm conformation) Method: EM (single particle) / Resolution: 3.71 Å 73777 9z2t EMDB-73777, PDB-9z2t: CryoEM structure of human NSUN2 with tRNA Lys(CTT) and SFG (No D-arm conformation) Method: EM (single particle) / Resolution: 3.7 Å 73778 9z2u EMDB-73778, PDB-9z2u: CryoEM structure of human NSUN2(C271A) with SAH cross-linked to tRNA Lys(TTT) (D-arm conformation) Method: EM (single particle) / Resolution: 3.0 Å 73780 9z2w EMDB-73780, PDB-9z2w: CryoEM structure of human NSUN2(C271A) with SAH cross-linked to tRNA Lys(TTT) (No D-arm conformation) Method: EM (single particle) / Resolution: 3.1 Å 73784 9z3d EMDB-73784, PDB-9z3d: CryoEM structure of human NSUN2(C271A) with SAH cross-linked to a pre-tRNA Leu(CAA) intron Method: EM (single particle) / Resolution: 2.96 Å
Chemicals	ChemComp-SAH: S-ADENOSYL-L-HOMOCYSTEINE ChemComp-SFG: SINEFUNGIN
Source	homo sapiens (human)
Keywords	TRANSFERASE / Methyltransferase / tRNA / Complex