7SVA

Cryo-EM structure of Arabidopsis Ago10-guide RNA complex

Summary for 7SVA

• Entry DOI: 10.2210/pdb7sva/pdb
• EMDB information: 25446
• Descriptor: Protein argonaute 10, RNA (5'-R(P*UP*GP*GP*AP*GP*UP*GP*UP*GP*AP*CP*AP*AP*UP*GP*GP*UP*GP*UP*UP*U)-3'), MAGNESIUM ION (3 entities in total)
• Functional Keywords: mirna, sirna, rna silencing, argonaute, plant, gene regulation
• Biological source: Arabidopsis thaliana (thale cress); More
• Total number of polymer chains: 2
• Total formula weight: 117793.96

Authors

Xiao, Y.,MacRae, I.J. (deposition date: 2021-11-18, release date: 2022-11-23, Last modification date: 2024-06-05)

Primary citation

Xiao, Y.,Maeda, S.,Otomo, T.,MacRae, I.J.
Structural basis for RNA slicing by a plant Argonaute.
Nat.Struct.Mol.Biol., 30:778-784, 2023

PubMed 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.

PubMed: 37127820
DOI: 10.1038/s41594-023-00989-7

Experimental method

ELECTRON MICROSCOPY (3.26 Å)