Summary information and primary citation
- PDB-id
- 7swq; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- gene regulation
- Method
- cryo-EM (3.79 Å)
- Summary
- cryo-EM structure of arabidopsis ago10-guide-target RNA complex in a bent duplex conformation
- Reference
- Xiao Y, Maeda S, Otomo T, MacRae IJ (2023): "Structural basis for RNA slicing by a plant Argonaute." Nat.Struct.Mol.Biol., 30, 778-784. doi: 10.1038/s41594-023-00989-7.
- Abstract
- Argonaute (AGO) proteins use small RNAs to recognize transcripts targeted for silencing in plants and animals. Many AGOs cleave target RNAs using an endoribonuclease activity termed 'slicing'. Slicing by DNA-guided prokaryotic AGOs has been studied in detail, but structural insights into RNA-guided slicing by eukaryotic AGOs are lacking. Here we present cryogenic electron microscopy structures of the Arabidopsis thaliana Argonaute10 (AtAgo10)-guide RNA complex with and without a target RNA representing a slicing substrate. The AtAgo10-guide-target complex adopts slicing-competent and slicing-incompetent conformations that are unlike known prokaryotic AGO structures. AtAgo10 slicing activity is licensed by docking target (t) nucleotides t9-t13 into a surface channel containing the AGO endoribonuclease active site. A β-hairpin in the L1 domain secures the t9-t13 segment and coordinates t9-t13 docking with extended guide-target pairing. Results show that prokaryotic and eukaryotic AGOs use distinct mechanisms for achieving target slicing and provide insights into small interfering RNA potency.