Summary information and primary citation
- PDB-id
-
1r9f;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- viral protein-RNA
- Method
- X-ray (1.85 Å)
- Summary
- Crystal structure of p19 complexed with 19-bp small
interfering RNA
- Reference
-
Ye K, Malinina L, Patel DJ (2003): "Recognition
of small interfering RNA by a viral suppressor of
RNA." Nature, 426, 874-878.
doi: 10.1038/nature02213.
- Abstract
- RNA silencing (also known as RNA interference) is a
conserved biological response to double-stranded RNA that
regulates gene expression, and has evolved in plants as a
defence against viruses. The response is mediated by small
interfering RNAs (siRNAs), which guide the
sequence-specific degradation of cognate messenger RNAs. As
a counter-defence, many viruses encode proteins that
specifically inhibit the silencing machinery. The p19
protein from the tombusvirus is such a viral suppressor of
RNA silencing and has been shown to bind specifically to
siRNA. Here, we report the 1.85-A crystal structure of p19
bound to a 21-nucleotide siRNA, where the 19-base-pair RNA
duplex is cradled within the concave face of a continuous
eight-stranded beta-sheet, formed across the p19 homodimer
interface. Direct and water-mediated intermolecular
contacts are restricted to the backbone phosphates and
sugar 2'-OH groups, consistent with sequence-independent
p19-siRNA recognition. Two alpha-helical 'reading heads'
project from opposite ends of the p19 homodimer and
position pairs of tryptophans for stacking over the
terminal base pairs, thereby measuring and bracketing both
ends of the siRNA duplex. Our structure provides an
illustration of siRNA sequestering by a viral protein.