› 4v2g

X-ray diffraction
2.71Å resolution

Tetracycline repressor TetR(D) bound to chlortetracycline and iso- chlortetracycline

Released:
DOI: 10.2210/pdb4v2g/pdb
PDB entry 4v2g coloured by chain, front view.
PDB entry 4v2g coloured by chain, side view.
PDB entry 4v2g coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Tetracycline repressor allostery does not depend on divalent metal recognition.
Werten S, Dalm D, Palm GJ, Grimm CC, Hinrichs W
Biochemistry 53 7990-8 (2014)
PMID: 25432019

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142298 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tetracycline repressor protein class D Chains: A, B
Molecule details ›
Chains: A, B
Length: 207 amino acids
Theoretical weight: 23.29 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P0ACT4 (Residues: 2-208; Coverage: 95%)
Gene name: tetR
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ITC 1 x ITC
Ligand CTC 1 x CTC
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P43212
Unit cell:
a: 69.249Å b: 69.249Å c: 182.373Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.175 0.252
Expression system: Escherichia coli K-12

Quick links

Citations

6 citation in other articles

Modular organisation of inducer recognition and allostery in the tetracycline repressor.
Werten et al. (2016)
5 more

1 mention without citation

Bifunctional optogenetic switch for improving shikimic acid production in E. coli.
Komera et al. (2022)