› 2mmh

Solution NMR

Unphosphorylated Mengovirus Leader Protein: NMR Studies of the Phosphorylation of the Mengovirus Leader Protein Reveal Stabilization of Intermolecular Domain Interactions

Released:
DOI: 10.2210/pdb2mmh/pdb
PDB entry 2mmh coloured by chain, ensemble of 10 models, front view.
PDB entry 2mmh coloured by chain, ensemble of 10 models, side view.
PDB entry 2mmh coloured by chain, ensemble of 10 models, top view.
Source organism: Mengo virus
Primary publication:
Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase.
Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC
Proc Natl Acad Sci U S A 111 15792-7 (2014)
PMID: 25331866

Function and Biology Details

Reactions catalysed: 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146131 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leader protein Chain: A
Molecule details ›
Chain: A
Length: 71 amino acids
Theoretical weight: 8.26 KDa
Source organism: Mengo virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12296 (Residues: 1-67; Coverage: 3%)
Sequence domains: Virion protein N terminal domain

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 48%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Nucleocytoplasmic Trafficking Perturbation Induced by Picornaviruses.
Lizcano-Perret et al. (2021)
1 more

1 mention without citation

Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase.
Bacot-Davis et al. (2014)