8AQ8

FAD-dependent monooxygenase from Stenotrophomonas maltophilia

This is a non-PDB format compatible entry.

Summary for 8AQ8

• Entry DOI: 10.2210/pdb8aq8/pdb
• Descriptor: Monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, 1,2-ETHANEDIOL, ... (8 entities in total)
• Functional Keywords: monooxygenase, fad-dependent, antibiotic resistance, oxidoreductase
• Biological source: Stenotrophomonas maltophilia
• Total number of polymer chains: 4
• Total formula weight: 160963.97

Authors

Maly, M.,Kolenko, P.,Duskova, J.,Skalova, T.,Dohnalek, J. (deposition date: 2022-08-11, release date: 2023-07-12, Last modification date: 2024-11-20)

Primary citation

Maly, M.,Kolenko, P.,Stransky, J.,Svecova, L.,Duskova, J.,Koval', T.,Skalova, T.,Trundova, M.,Adamkova, K.,Cerny, J.,Bozikova, P.,Dohnalek, J.
Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia.
Acta Crystallogr.,Sect.F, 79:180-192, 2023

PubMed 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.

PubMed: 37405486
DOI: 10.1107/S2053230X23005381

Experimental method

X-RAY DIFFRACTION (1.95 Å)