36PD image
Deposition Date 2026-06-24
Release Date 2026-09-16
Last Version Date 2026-11-04
Entry Detail
PDB ID:
36PD
Title:
P. fulva VIPR Ternary Complex with four subunits
Biological Source:
Source Organism(s):
Expression System(s):
Method Details:
Experimental Method:
Resolution:
2.80 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Structural Superimposition Protein Blast
Polymer Type:polypeptide(L)
Molecule:Vipr protein
Chain IDs:A, B, C, D
Chain Length:212
Number of Molecules:4
Biological Source:Pseudomonas fulva
Polymer Type:polydeoxyribonucleotide
Molecule:Target Strand
Chain IDs:E (auth: K)
Chain Length:12
Number of Molecules:1
Biological Source:Escherichia coli
Polymer Type:polyribonucleotide
Molecule:viprRNA
Chain IDs:F (auth: L)
Chain Length:20
Number of Molecules:1
Biological Source:Pseudomonas fulva
Primary Citation
VIPR RNA-guided DNA recognition by noncontiguous geometric triplex formation.
Science 393 1236 1240 (2026)
PMID: 42752121 DOI: 10.1126/science.aei3472

Abstact

Viral interference programmable repeat (VIPR) systems use a noncontiguous code for RNA-guided transcriptional silencing. How the Vipr protein and a VIPR RNA (vrRNA) comprising alternating GGY and NN segments achieve precise DNA targeting is unknown. Here, we present 21 cryo-electron microscopy structures that help explain the mechanism of target engagement. Vipr protomers oligomerize along the vrRNA to form a right-handed helical filament, sequestering each GGY motif and positioning the adjacent NN bases for target base pairing. DNA binding, in which every third nucleotide is skipped, results in a gapped vrRNA-DNA hybrid helix that encircles the nontarget DNA strand to form a geometric triplex. These findings suggest that triplex-mediated target-strand handoff could enable noncontiguous and programmable RNA-guided DNA recognition in VIPR systems.

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Primary Citation of related structures
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