X-ray diffraction
2.5Å resolution

Crystal structures and functional analysis of murine norovirus RNA-dependent RNA polymerase

Source organism: Murine norovirus 1
Primary publication:
Crystal structures of murine norovirus-1 RNA-dependent RNA polymerase.
J. Gen. Virol. 92 1607-16 (2011)
PMID: 21471315

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|- and the P1' position is occupied by Gly-|-
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
NTPase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 517 amino acids
Theoretical weight: 58.52 KDa
Source organism: Murine norovirus 1
Expression system: Escherichia coli
  • Canonical: Q80J95 (Residues: 1181-1686; Coverage: 30%)
Sequence domains: Viral RNA-dependent RNA polymerase
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: C2
Unit cell:
a: 120.557Å b: 196.262Å c: 109.339Å
α: 90° β: 114.23° γ: 90°
R R work R free
0.202 0.199 0.245
Expression system: Escherichia coli