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     margin-left: 10px;  }  @media (max-width: 600px) {    .kudos-widget .kudos-widget-article .kudos-box-with-avatar > ul > li.group-of-authors {      background-image:none!important;      background-size:0 0;      padding-left:10px;      min-height:0;    }  }</style><div class="kudos-widget ng-non-bindable" ngNonBindable>   <div class="kudos-widget-article">    <div class="kudos-widget-intro-and-logo">      <a target="_blank" href="https://www.growkudos.com/"><img src="https://api.growkudos.com/logo" alt="Kudos Logo" class="kudos-widget-article-logo-img"/></a>    </div>    <div>      <h1 class="kudos-article-title">        Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia      </h1>    </div>          <div class="kudos-box kudos-box-with-avatar">        <h3>What is it about?</h3>          <div class="wrap-words">            <p class="preserve-line-breaks">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.</p>          </div>      </div>              <div class="kudos-box kudos-box-with-avatar">        <h3>          Why is it important?        </h3>          <div class="wrap-words">            <p class="preserve-line-breaks">Our results provide evidence that S. maltophilia codes for an enzyme that is capable of degrading tetracycline antibiotics, even if such a mechanism is not essential for its resistance to these antibiotics.</p>          </div>        </div>                      <div class="kudos-widget-article-readmore-btn-container">        <a class="btn btn-md btn-block blue-background" target="_blank" href="https://www.growkudos.com/articles/10.1107/s2053230x23005381?utm_medium=widget&amp;utm_source=publication-widget">Read more on Kudos&hellip;</a>      </div>            <div class="with-bottom-small-margin">        <div class="inline-block">          The following have contributed to this page:        </div>        <div class="inline-block">          Martin MalĂ˝        </div>      </div>  </div></div>' ,"url"));