Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia.

Autor: Malý M; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Kolenko P; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Stránský J; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Švecová L; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Dušková J; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Koval' T; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Skálová T; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Trundová M; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Adámková K; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Černý J; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Božíková P; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic., Dohnálek J; Institute of Biotechnology, Czech Academy of Sciences, v.v.i., BIOCEV, Průmyslová 595, 252 50 Vestec, Czech Republic.
Jazyk: angličtina
Zdroj: Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2023 Jul 01; Vol. 79 (Pt 7), pp. 180-192. Date of Electronic Publication: 2023 Jul 05.
DOI: 10.1107/S2053230X23005381
Abstrakt: 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.
(open access.)
Databáze: MEDLINE
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