4v9e

X-ray diffraction
3.4Å resolution

Crystal Structure of Rift Valley Fever Virus Nucleocapsid Protein Hexamer 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 heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112513 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Nucleoprotein Chains: AA, AB, AC, AD, AE, AF, AG, AH, AI, AJ, AK, AL, AM, AN, AO, AP, AQ, AR, BA, BB, BC, BD, BE, BF, BG, BH, BI, BJ, BK, BL, BM, BN, BO, BP, BQ, BR
Molecule details ›
Chains: AA, AB, AC, AD, AE, AF, AG, AH, AI, AJ, AK, AL, AM, AN, AO, AP, AQ, AR, BA, BB, BC, BD, BE, BF, BG, BH, BI, BJ, BK, BL, BM, BN, BO, BP, BQ, BR
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: Aa, Ag, Am, Ba, Bg, Bm
Molecule details ›
Chains: Aa, Ag, Am, Ba, Bg, Bm
Length: 36 nucleotides
Theoretical weight: 10.98 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: 91.66Å b: 173.33Å c: 172.9Å
α: 119.95° β: 99.34° γ: 90.12°
R-values:
R R work R free
0.225 0.225 0.24
Expression systems:
  • Escherichia coli BL21
  • Not provided