› 5tul

X-ray diffraction
2Å resolution

Crystal structure of tetracycline destructase Tet(55)

Released:
DOI: 10.2210/pdb5tul/pdb
PDB entry 5tul coloured by chain, front view.
PDB entry 5tul coloured by chain, side view.
PDB entry 5tul coloured by chain, top view.
Source organism: uncultured bacterium
Primary publication:
Plasticity, dynamics, and inhibition of emerging tetracycline resistance enzymes.
Park J, Gasparrini AJ, Reck MR, Symister CT, Elliott JL, Vogel JP, Wencewicz TA, Dantas G, Tolia NH
OpenAccess logo Nat Chem Biol 13 730-736 (2017)
PMID: 28481346

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102199 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavin-dependent monooxygenase Chain: A
Molecule details ›
Chain: A
Length: 406 amino acids
Theoretical weight: 45.33 KDa
Source organism: uncultured bacterium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H4TXY1 (Residues: 1-385; Coverage: 100%)
Gene name: tet(55)
Sequence domains: FAD binding domain

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21212
Unit cell:
a: 64.74Å b: 124.41Å c: 45.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.192 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Ribosome-Targeting Antibiotics: Modes of Action, Mechanisms of Resistance, and Implications for Drug Design.
Lin et al. (2018)
14 more

2 mentions without citation

Plasticity, dynamics, and inhibition of emerging tetracycline resistance enzymes.
Park et al. (2017)
1 more