Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia

Acta Crystallogr F Struct Biol Commun. 2023 Jul 1;79(Pt 7):180-192. doi: 10.1107/S2053230X23005381. Epub 2023 Jul 5.

Abstract

The resistance of the emerging human pathogen Stenotrophomonas maltophilia to tetracycline antibiotics mainly depends on multidrug efflux pumps and ribosomal protection enzymes. However, the genomes of several strains of this Gram-negative bacterium code for a FAD-dependent monooxygenase (SmTetX) homologous to tetracycline destructases. This protein was recombinantly produced and its structure and function were investigated. Activity assays using SmTetX showed its ability to modify oxytetracycline with a catalytic rate comparable to those of other destructases. SmTetX shares its fold with the tetracycline destructase TetX from Bacteroides thetaiotaomicron; however, its active site possesses an aromatic region that is unique in this enzyme family. A docking study confirmed tetracycline and its analogues to be the preferred binders amongst various classes of antibiotics.

Keywords: FAD-dependent monooxygenases; antibiotic resistance; tetracycline.

MeSH terms

  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology
  • Crystallography, X-Ray
  • Humans
  • Microbial Sensitivity Tests
  • Oxytetracycline* / metabolism
  • Stenotrophomonas maltophilia* / genetics
  • Stenotrophomonas maltophilia* / metabolism
  • Tetracycline / metabolism
  • Tetracycline / pharmacology

Substances

  • Anti-Bacterial Agents
  • Tetracycline
  • Oxytetracycline