Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia

0574533 - BTÚ 2024 RIV US eng J - Článek v odborném periodiku
Malý, Martin - Kolenko, Petr - Stránský, Jan - Švecová, Leona - Dušková, Jarmila - Koval, Tomáš - Skálová, Tereza - Trundová, Mária - Adámková, Kristýna - Černý, Jiří - Božíková, Paulina - Dohnálek, Jan
Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia.
Acta Crystallographica Section F-Structural Biology and Crystallization Communications. Roč. 79, JUL 2023 (2023), s. 180-192. ISSN 1744-3091. E-ISSN 2053-230X
Grant CEP: GA MŠMT EF16_019/0000778; GA MŠMT EF15_003/0000447; GA MŠMT(CZ) ED1.1.00/02.0109; GA MŠMT(CZ) EF18_046/0015974
Výzkumná infrastruktura: CIISB III - 90242
Institucionální podpora: RVO:86652036
Klíčová slova: FAD-dependent monooxygenases * tetracycline * antibiotic resistance
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 0.9, rok: 2022
Způsob publikování: Open access
https://scripts.iucr.org/cgi-bin/paper?S2053230X23005381

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.
Trvalý link: https://hdl.handle.net/11104/0346203