1R4K

Solution Structure of the Drosophila Argonaute 1 PAZ Domain

Summary for 1R4K

• Entry DOI: 10.2210/pdb1r4k/pdb
• Descriptor: Argonaute 1 (1 entity in total)
• Functional Keywords: beta barrel, rna binding protein
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 19799.15

Authors

Yan, K.S.,Yan, S.,Farooq, A.,Han, A.,Zeng, L.,Zhou, M.-M. (deposition date: 2003-10-07, release date: 2003-12-09, Last modification date: 2024-05-22)

Primary citation

Yan, K.S.,Yan, S.,Farooq, A.,Han, A.,Zeng, L.,Zhou, M.-M.
Structure and conserved RNA binding of the PAZ domain
Nature, 426:468-474, 2003

PubMed Abstract: The discovery of RNA-mediated gene-silencing pathways, including RNA interference, highlights a fundamental role of short RNAs in eukaryotic gene regulation and antiviral defence. Members of the Dicer and Argonaute protein families are essential components of these RNA-silencing pathways. Notably, these two families possess an evolutionarily conserved PAZ (Piwi/Argonaute/Zwille) domain whose biochemical function is unknown. Here we report the nuclear magnetic resonance solution structure of the PAZ domain from Drosophila melanogaster Argonaute 1 (Ago1). The structure consists of a left-handed, six-stranded beta-barrel capped at one end by two alpha-helices and wrapped on one side by a distinctive appendage, which comprises a long beta-hairpin and a short alpha-helix. Using structural and biochemical analyses, we demonstrate that the PAZ domain binds a 5-nucleotide RNA with 1:1 stoichiometry. We map the RNA-binding surface to the open face of the beta-barrel, which contains amino acids conserved within the PAZ domain family, and we define the 5'-to-3' orientation of single-stranded RNA bound within that site. Furthermore, we show that PAZ domains from different human Argonaute proteins also bind RNA, establishing a conserved function for this domain.

PubMed: 14615802
DOI: 10.1038/nature02129

Experimental method

SOLUTION NMR