› 6gpg

X-ray diffraction
2.89Å resolution

Structure of the RIG-I Singleton-Merten syndrome variant C268F

Released:
DOI: 10.2210/pdb6gpg/pdb
PDB entry 6gpg coloured by chain, front view.
PDB entry 6gpg coloured by chain, side view.
PDB entry 6gpg coloured by chain, top view.
Source organisms:
Primary publication:
Unified mechanisms for self-RNA recognition by RIG-I Singleton-Merten syndrome variants.
Lässig C, Lammens K, Gorenflos López JL, Michalski S, Fettscher O, Hopfner KP
Elife 7 (2018)
PMID: 30047865

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132026 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Antiviral innate immune response receptor RIG-I Chain: A
Molecule details ›
Chain: A
Length: 714 amino acids
Theoretical weight: 81.9 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: O95786 (Residues: 232-925; Coverage: 75%)
Gene names: DDX58, RIGI
Sequence domains:
Structure domains:
RNA (5'-R(*CP*GP*AP*CP*GP*CP*UP*AP*GP*CP*GP*UP*CP*G)-3') Chains: B, C
Molecule details ›
Chains: B, C
Length: 14 nucleotides
Theoretical weight: 4.48 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P6522
Unit cell:
a: 175.62Å b: 175.62Å c: 109.53Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.21 0.26
Expression systems:
  • Trichoplusia ni
  • Not provided

Quick links

Citations

8 review citations

The molecular mechanism of RIG-I activation and signaling.
Thoresen et al. (2021)
7 more

3 mentions without citation

Host DDX Helicases as Possible SARS-CoV-2 Proviral Factors: A Structural Overview of Their Hijacking Through Multiple Viral Proteins.
Squeglia et al. (2020)
2 more