4G0Y

Crystal structure of Arabidopsis AGO1 in complex with AMP

Summary for 4G0Y

• Entry DOI: 10.2210/pdb4g0y/pdb
• Related: 4G0M 4G0O 4G0P 4G0Q 4G0X 4G0Z
• Descriptor: Protein argonaute 1, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: mid domain, gene regulation
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Cytoplasm (Potential): O04379
• Total number of polymer chains: 1
• Total formula weight: 16786.38

Authors

Frank, F.,Hauver, J.,Sonenberg, N.,Nagar, B. (deposition date: 2012-07-10, release date: 2012-07-25, Last modification date: 2024-02-28)

Primary citation

Frank, F.,Hauver, J.,Sonenberg, N.,Nagar, B.
Arabidopsis Argonaute MID domains use their nucleotide specificity loop to sort small RNAs.
Embo J., 31:3588-3595, 2012

PubMed Abstract: The 5'-nucleotide of small RNAs associates directly with the MID domain of Argonaute (AGO) proteins. In humans, the identity of the 5'-base is sensed by the MID domain nucleotide specificity loop and regulates the integrity of miRNAs. In Arabidopsis thaliana, the 5'-nucleotide also controls sorting of small RNAs into the appropriate member of the AGO family; however, the structural basis for this mechanism is unknown. Here, we present crystal structures of the MID domain from three Arabidopsis AGOs, AtAGO1, AtAGO2 and AtAGO5, and characterize their interactions with nucleoside monophosphates (NMPs). In AtAGOs, the nucleotide specificity loop also senses the identity of the 5'-nucleotide but uses more diverse modes of recognition owing to the greater complexity of small RNAs found in plants. Binding analyses of these interactions reveal a strong correlation between their affinities and evolutionary conservation.

PubMed: 22850669
DOI: 10.1038/emboj.2012.204

Experimental method

X-RAY DIFFRACTION (1.65 Å)