Summary information and primary citation
- PDB-id
- 2xfm; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- RNA-protein
- Method
- NMR
- Summary
- Complex structure of the miwi paz domain bound to methylated single stranded RNA
- Reference
- Simon B, Kirkpatrick JP, Eckhardt S, Reuter M, Rocha EA, Andrade-Navarro MA, Sehr P, Pillai RS, Carlomagno T (2011): "Recognition of 2'-O-Methylated 3'-End of Pirna by the Paz Domain of a Piwi Protein." Structure, 19, 172. doi: 10.1016/J.STR.2010.11.015.
- Abstract
- Piwi proteins are germline-specific Argonautes that associate with small RNAs called Piwi-interacting RNAs (piRNAs), and together with these RNAs are implicated in transposon silencing. The PAZ domain of Argonaute proteins recognizes the 3'-end of the RNA, which in the case of piRNAs is invariably modified with a 2'-O-methyl group. Here, we present the solution structure of the PAZ domain from the mouse Piwi protein, MIWI, in complex with an 8-mer piRNA mimic. The methyl group is positioned in a hydrophobic cavity made of conserved amino acids from strand β7 and helix α3, where it is contacted by the side chain of methionine-382. Our structure is similar to that of Ago-PAZ, but subtle differences illustrate how the PAZ domain has evolved to accommodate distinct 3' ends from a variety of RNA substrates.
