1r4k
From Proteopedia
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Solution Structure of the Drosophila Argonaute 1 PAZ Domain
Overview
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.
About this Structure
1R4K is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Structure and conserved RNA binding of the PAZ domain., Yan KS, Yan S, Farooq A, Han A, Zeng L, Zhou MM, Nature. 2003 Nov 27;426(6965):468-74. Epub 2003 Nov 16. PMID:14615802
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