1RPU

Crystal Structure of CIRV p19 bound to siRNA

Summary for 1RPU

• Entry DOI: 10.2210/pdb1rpu/pdb
• Descriptor: 5'-R(P*CP*GP*UP*AP*CP*GP*CP*GP*UP*CP*AP*CP*GP*CP*GP*UP*AP*CP*GP*UP*U)-3', 19 kDa protein (3 entities in total)
• Functional Keywords: rnai, protein-rna complex, rna double helix, rna length recognition, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Carnation Italian ringspot virus; More
• Total number of polymer chains: 4
• Total formula weight: 52078.74

Authors

Vargason, J.M.,Szittya, G.,Burgyan, J.,Hall, T.M.T. (deposition date: 2003-12-03, release date: 2004-01-13, Last modification date: 2024-02-14)

Primary citation

Vargason, J.M.,Szittya, G.,Burgyan, J.,Hall, T.M.T.
Size selective recognition of siRNA by an RNA silencing suppressor
Cell(Cambridge,Mass.), 115:799-811, 2003

PubMed Abstract: RNA silencing in plants likely exists as a defense mechanism against molecular parasites such as RNA viruses, retrotransposons, and transgenes. As a result, many plant viruses have adapted mechanisms to evade and suppress gene silencing. Tombusviruses express a 19 kDa protein (p19), which has been shown to suppress RNA silencing in vivo and bind silencing-generated and synthetic small interfering RNAs (siRNAs) in vitro. Here we report the 2.5 A crystal structure of p19 from the Carnation Italian ringspot virus (CIRV) bound to a 21 nt siRNA and demonstrate in biochemical and in vivo assays that CIRV p19 protein acts as a molecular caliper to specifically select siRNAs based on the length of the duplex region of the RNA.

PubMed: 14697199
DOI: 10.1016/S0092-8674(03)00984-X

Experimental method

X-RAY DIFFRACTION (2.5 Å)