› 2xge

X-ray diffraction
2.14Å resolution

Crystal structure of a designed heterodimeric variant T-A(A)B of the tetracycline repressor

Released:
DOI: 10.2210/pdb2xge/pdb
PDB entry 2xge coloured by chain, front view.
PDB entry 2xge coloured by chain, side view.
PDB entry 2xge coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Computational design of a chain-specific tetracycline repressor heterodimer.
Stiebritz MT, Wengrzik S, Klein DL, Richter JP, Srebrzynski A, Weiler S, Muller YA
J Mol Biol 403 371-85 (2010)
PMID: 20816982

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-137865 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tetracycline repressor protein class B from transposon Tn10; Tetracycline repressor protein class D Chain: A
Molecule details ›
Chain: A
Length: 208 amino acids
Theoretical weight: 23.44 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P04483 (Residues: 1-56; Coverage: 27%)
  • Canonical: P0ACT4 (Residues: 57-208; Coverage: 70%)
Gene name: tetR
Sequence domains:
Structure domains:
Tetracycline repressor protein class B from transposon Tn10; Tetracycline repressor protein class D Chain: B
Molecule details ›
Chain: B
Length: 211 amino acids
Theoretical weight: 23.71 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P04483 (Residues: 1-56; Coverage: 27%)
  • Canonical: P0ACT4 (Residues: 57-208; Coverage: 70%)
Gene name: tetR
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand EDO 1 x EDO
Ligand NA 1 x NA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I4122
Unit cell:
a: 69.127Å b: 69.127Å c: 182.949Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.205 0.26
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Status quo of tet regulation in bacteria.
Bertram et al. (2022)
4 other articles

1 mention without citation

Ultratight crystal packing of a 10 kDa protein.
Trillo-Muyo et al. (2013)