› 1cei

X-ray diffraction
1.8Å resolution

STRUCTURE DETERMINATION OF THE COLICIN E7 IMMUNITY PROTEIN (IMME7) THAT BINDS SPECIFICALLY TO THE DNASE-TYPE COLICIN E7 AND INHIBITS ITS BACTERIOCIDAL ACTIVITY

Released:
DOI: 10.2210/pdb1cei/pdb
PDB entry 1cei coloured by chain, front view.
PDB entry 1cei coloured by chain, side view.
PDB entry 1cei coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structure of the immunity protein of colicin E7 suggests a possible colicin-interacting surface.
Chak KF, Safo MK, Ku WY, Hsieh SY, Yuan HS
Proc Natl Acad Sci U S A 93 6437-42 (1996)
PMID: 8692833

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169935 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Colicin-E7 immunity protein Chain: A
Molecule details ›
Chain: A
Length: 94 amino acids
Theoretical weight: 10.65 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: Q03708 (Residues: 1-87; Coverage: 100%)
Gene names: ceiE7, imm
Sequence domains: Colicin immunity protein / pyocin immunity protein
Structure domains: Colicin E immunity protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: I222
Unit cell:
a: 75.14Å b: 50.48Å c: 45.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 not available

Quick links

Citations

3 review citations

Molecular mechanisms of bacteriocin evolution.
Riley MA. (1998)
2 more

17 mentions without citation

An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state.
Zhang et al. (2004)
16 more