› 2xdo

X-ray diffraction
2.09Å resolution

Structure of the Tetracycline degrading Monooxygenase TetX2 from Bacteroides thetaiotaomicron

Released:
DOI: 10.2210/pdb2xdo/pdb
PDB entry 2xdo coloured by chain, front view.
PDB entry 2xdo coloured by chain, side view.
PDB entry 2xdo coloured by chain, top view.
Source organism: Bacteroides thetaiotaomicron
Primary publication:
Structural basis for a new tetracycline resistance mechanism relying on the TetX monooxygenase.
Volkers G, Palm GJ, Weiss MS, Wright GD, Hinrichs W
FEBS Lett 585 1061-6 (2011)
PMID: 21402075

Function and Biology Details

Reaction catalysed: 
Tetracycline + NADPH + O(2) = 11a-hydroxytetracycline + NADP(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188092 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavin-dependent monooxygenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 398 amino acids
Theoretical weight: 44.7 KDa
Source organism: Bacteroides thetaiotaomicron
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93L51 (Residues: 11-388; Coverage: 97%)
Gene name: tetX2
Sequence domains: FAD binding domain
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
1 bound ligand:
Ligand SO4 13 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.3
Spacegroup: P1
Unit cell:
a: 68.11Å b: 80.27Å c: 86.89Å
α: 111° β: 90.23° γ: 93.43°
R-values:
R R work R free
0.192 0.19 0.23
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

Ribosome-targeting antibiotics and mechanisms of bacterial resistance.
Wilson DN. (2014)
11 more

5 mentions without citation

The role of adjuvants in overcoming antibacterial resistance due to enzymatic drug modification.
El-Khoury et al. (2022)
4 more