Structures of FOX-4 Cephamycinase in Complex with Transition-State Analog Inhibitors.
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ABSTRACT:
SUBMITTER: Lefurgy ST
PROVIDER: S-EPMC7277225 | biostudies-literature | 2020 Apr
REPOSITORIES: biostudies-literature
Publications
Structures of FOX-4 Cephamycinase in Complex with Transition-State Analog Inhibitors.
Lefurgy Scott T ST Caselli Emilia E Taracila Magdalena A MA Malashkevich Vladimir N VN Biju Beena B Papp-Wallace Krisztina M KM Bonanno Jeffrey B JB Prati Fabio F Almo Steven C SC Bonomo Robert A RA
Biomolecules 20200427 5
Boronic acid transition-state analog inhibitors (BATSIs) are partners with β-lactam antibiotics for the treatment of complex bacterial infections. Herein, microbiological, biochemical, and structural findings on four BATSIs with the FOX-4 cephamycinase, a class C β-lactamase that rapidly hydrolyzes cefoxitin, are revealed. FOX-4 is an extended-spectrum class C cephalosporinase that demonstrates conformational flexibility when complexed with certain ligands. Like other β-lactamases of this class, ...[more]
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