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Solution NMR

Solution structure of the E. coli bacteriophage P1 encoded HOT protein: a homologue of the theta subunit of E. coli DNA polymerase III

Released:
DOI: 10.2210/pdb1se7/pdb
PDB entry 1se7 coloured by chain, ensemble of 7 models, front view.
PDB entry 1se7 coloured by chain, ensemble of 7 models, side view.
PDB entry 1se7 coloured by chain, ensemble of 7 models, top view.
Source organism: Escherichia virus P1
Primary publication:
Phage like it HOT: solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the theta subunit of E. coli DNA polymerase III.
Derose EF, Kirby TW, Mueller GA, Chikova AK, Schaaper RM, London RE
Structure 12 2221-31 (2004)
PMID: 15576035

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180761 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hot Chain: A
Molecule details ›
Chain: A
Length: 83 amino acids
Theoretical weight: 9.71 KDa
Source organism: Escherichia virus P1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q71T70 (Residues: 5-87; Coverage: 95%)
Gene name: hot
Sequence domains: DNA polymerase III, theta subunit
Structure domains: DNA polymerase III-theta

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, molecular dynamics, torsion angle dynamics
Expression system: Escherichia coli

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Citations

8 citation in other articles

Modulation of the W748S mutation in DNA polymerase gamma by the E1143G polymorphismin mitochondrial disorders.
Chan et al. (2006)
7 more

6 mentions without citation

Protein-protein docking benchmark version 4.0.
Hwang et al. (2010)
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