4h5o

X-ray diffraction
3.9Å resolution

Crystal Structure of Rift Valley Fever Virus Nucleocapsid Protein Pentamer Bound to Single-stranded RNA

Released:
Source organism: Rift Valley fever virus
Primary publication:
Phleboviruses encapsidate their genomes by sequestering RNA bases.
Proc Natl Acad Sci U S A 109 19208-13 (2012)
PMID: 23129612

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112510 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Nucleoprotein Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 245 amino acids
Theoretical weight: 27.37 KDa
Source organism: Rift Valley fever virus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: D3K5I7 (Residues: 1-245; Coverage: 100%)
Gene name: N
Sequence domains: Tenuivirus/Phlebovirus nucleocapsid protein
35-mer poly(U) RNA Chains: K, L
Molecule details ›
Chains: K, L
Length: 35 nucleotides
Theoretical weight: 10.67 KDa
Source organism: Rift Valley fever virus
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P1
Unit cell:
a: 79.81Å b: 93.59Å c: 124.78Å
α: 101.7° β: 90.27° γ: 114.18°
R-values:
R R work R free
0.229 0.228 0.248
Expression systems:
  • Escherichia coli BL21
  • Not provided