› 2vhq

X-ray diffraction
2.15Å resolution

P4 PROTEIN FROM BACTERIOPHAGE PHI12 S252A mutant in complex with ATP AND MG

Released:
DOI: 10.2210/pdb2vhq/pdb
PDB entry 2vhq coloured by chain, front view.
PDB entry 2vhq coloured by chain, side view.
PDB entry 2vhq coloured by chain, top view.
Source organism: Pseudomonas phage phi12
Primary publication:
Structural basis of mechanochemical coupling in a hexameric molecular motor.
Kainov DE, Mancini EJ, Telenius J, Lísal J, Grimes JM, Bamford DH, Stuart DI, Tuma R
J Biol Chem 283 3607-3617 (2008)
PMID: 18057007

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188245 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NTPase P4 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 331 amino acids
Theoretical weight: 35.13 KDa
Source organism: Pseudomonas phage phi12
Expression system: Escherichia coli
UniProt:
  • Canonical: Q94M05 (Residues: 1-331; Coverage: 100%)
Gene name: 4
Sequence domains: ATPase P4 of dsRNA bacteriophage phi-12
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ATP 3 x ATP
Ligand MG 3 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: I222
Unit cell:
a: 105.244Å b: 129.387Å c: 158.978Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.247
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Biophysics of viral infectivity: matching genome length with capsid size.
Nurmemmedov et al. (2007)
3 more

1 mention without citation

Distinct Conformation of ATP Molecule in Solution and on Protein.
Kobayashi et al. (2013)