Structural and biochemical analysis of the metallo-β-lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di-metal scaffold for catalytic activity.

ABSTRACT: Emergence of Enterobacteriaceae harboring metallo-β-lactamases (MBL) has raised global threats due to their broad antibiotic resistance profiles and the lack of effective inhibitors against them. We have been studied one of the emerging environmental MBL, the L1 from Stenotrophomonas maltophilia K279a. We determined several crystal structures of L1 complexes with three different classes of β-lactam antibiotics (penicillin G, moxalactam, meropenem, and imipenem), with the inhibitor captopril and different metal ions (Zn⁺² , Cd⁺² , and Cu⁺² ). All hydrolyzed antibiotics and the inhibitor were found binding to two Zn⁺² ions mainly through the opened lactam ring and some hydrophobic interactions with the binding pocket atoms. Without a metal ion, the

SUBMITTER: Kim Y 

PROVIDER: S-EPMC7020990 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature