RNA silencing suppressor p19. Chain: a, b. Synonym: 19 kda symptom severity modulator. Engineered: yes. Mutation: yes. RNA (5'- r(p Up Cp Gp Ap Ap Gp Up Ap Up Up Cp Cp Gp Cp Gp Up Ap Cp Gp Up U)- 3'). Chain: c.
D.V.Foss
et al.
(2019).
Structural insights into interactions between viral suppressor of RNA silencing protein p19 mutants and small RNAs.
FEBS Open Bio,
9,
1042-1051.
PubMed id: 31021526
DOI: 10.1002/2211-5463.12644
Date:
06-Nov-17
Release date:
16-Jan-19
PROCHECK
Headers
References
Protein chains
Q66104 (P19_CIRV) -
RNA silencing suppressor p19 from Carnation Italian ringspot virus
Seq: Struc:
172 a.a.
143 a.a.*
Key:
Secondary structure
*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
Structural insights into interactions between viral suppressor of RNA silencing protein p19 mutants and small RNAs.
D.V.Foss,
N.T.Schirle,
I.J.MacRae,
J.P.Pezacki.
ABSTRACT
Viral suppressors of RNA silencing (VSRSs) are a diverse group of viral proteins
that have evolved to disrupt eukaryotic RNA silencing pathways, thereby
contributing to viral pathogenicity. The p19 protein is a VSRS that selectively
binds to short interfering RNAs (siRNAs) over microRNAs (miRNAs). Mutational
analysis has identified single amino acid substitutions that reverse this
selectivity through new high-affinity interactions with human miR-122. Herein,
we report crystal structures of complexed p19-T111S (2.6 Å), p19-T111H (2.3 Å)
and wild-type p19 protein (2.2 Å) from the Carnation Italian ringspot virus
with small interfering RNA (siRNA) ligands. Structural comparisons reveal that
these mutations do not lead to major changes in p19 architecture, but instead
promote subtle rearrangement of residues and solvent molecules along the p19
midline. These observations suggest p19 uses many small interactions to
distinguish siRNAs from miRNAs and perturbing these interactions can create p19
variants with novel RNA-recognition properties. DATABASE: Model data are
deposited in the PDB database under the accession numbers 6BJG, 6BJH and 6BJV.