› 4g7x

X-ray diffraction
1.44Å resolution

Crystal structure of a complex between the CTXphi pIII N-terminal domain and the Vibrio cholerae TolA C-terminal domain

Released:
DOI: 10.2210/pdb4g7x/pdb
PDB entry 4g7x coloured by chain, front view.
PDB entry 4g7x coloured by chain, side view.
PDB entry 4g7x coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structures of a CTXphi pIII domain unbound and in complex with a Vibrio cholerae TolA domain reveal novel interaction interfaces.
Ford CG, Kolappan S, Phan HT, Waldor MK, Winther-Larsen HC, Craig L
J Biol Chem 287 36258-72 (2012)
PMID: 22942280

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101774 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Putative uncharacterized protein Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.51 KDa
Source organism: Vibrio cholerae CIRS101
Expression system: Escherichia coli
Structure domains: Vibrio phage CTXphi pIII, N-terminal N1 domain
TolA protein Chain: B
Molecule details ›
Chain: B
Length: 138 amino acids
Theoretical weight: 15.07 KDa
Source organism: Vibrio cholerae O395
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3AIH3 (Residues: 241-356; Coverage: 33%)
Gene names: VC0395_A1430, tolA
Sequence domains: TolA C-terminal
Structure domains: Fusion Protein Consisting Of Minor Coat Protein, Glycine Rich Linker, Tola, And A His Tag; Chain: A; Domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 43.38Å b: 46.16Å c: 101.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.216
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Colicin A binds to a novel binding site of TolA in the Escherichia coli periplasm.
Penfold et al. (2012)
8 other articles

6 mentions without citation

Force-Generation by the Trans-Envelope Tol-Pal System.
Webby et al. (2022)
5 more