2XFM

Complex structure of the MIWI Paz domain bound to methylated single stranded RNA

Summary for 2XFM

• Entry DOI: 10.2210/pdb2xfm/pdb
• Descriptor: PIWI-LIKE PROTEIN 1, 5'-R(*AP*CP*CP*GP*AP*CP*UP*(OMU)P)-3' (2 entities in total)
• Functional Keywords: rna-protein complex, differentiation, rna interference, rna/protein
• Biological source: MUS MUSCULUS (MOUSE); More
• Cellular location: Cytoplasm: Q9JMB7
• Total number of polymer chains: 2
• Total formula weight: 20141.63

Authors

Simon, B.,Kirkpatrick, J.P.,Eckhardt, S.,Sehr, P.,Andrade-Navarro, M.A.,Pillai, R.S.,Carlomagno, T. (deposition date: 2010-05-27, release date: 2011-01-26, Last modification date: 2024-05-15)

Primary citation

Simon, B.,Kirkpatrick, J.P.,Eckhardt, S.,Reuter, M.,Rocha, E.A.,Andrade-Navarro, M.A.,Sehr, P.,Pillai, R.S.,Carlomagno, T.
Recognition of 2'-O-Methylated 3'-End of Pirna by the Paz Domain of a Piwi Protein.
Structure, 19:172-, 2011

PubMed 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.

PubMed: 21237665
DOI: 10.1016/J.STR.2010.11.015

Experimental method

SOLUTION NMR