1RPU: Crystal Structure Of Cirv P19 Bound To Sirna

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.
PDB ID: 1RPUDownload
MMDB ID: 74247
PDB Deposition Date: 2003/12/3
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Carnation Italian ringspot virus
Similar Structures:
Biological Unit for 1RPU: tetrameric; determined by author
Molecular Components in 1RPU
Label Count Molecule
Proteins (2 molecules)
19 KDA Protein(Gene symbol: orf5)
Molecule annotation
Nucleotide(1 molecule)
5'-r(p*cp*gp*up*ap*cp*gp*cp*gp*up*cp*ap*cp*gp*cp*gp*up*ap*c P*gp*up*u)-3'
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB