Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F23%3A00574533" target="_blank" >RIV/86652036:_____/23:00574533 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22330/23:43926895

Výsledek na webu

<a href="https://scripts.iucr.org/cgi-bin/paper?S2053230X23005381" target="_blank" >https://scripts.iucr.org/cgi-bin/paper?S2053230X23005381</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S2053230X23005381" target="_blank" >10.1107/S2053230X23005381</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Crystallographica Section F-Structural Biology and Crystallization Communications

ISSN

1744-3091

e-ISSN

2053-230X

Svazek periodika

79

Číslo periodika v rámci svazku

JUL 2023

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

180-192

Kód UT WoS článku

001028861900003

EID výsledku v databázi Scopus

2-s2.0-85164256669