ArticleAntimicrobial agents and chemotherapy2016
Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.
Article in Antimicrobial agents and chemotherapy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- Biochemical properties and substrate specificity of GOB-38 in Elizabethkingia anophelis.Scientific reports · 2025Article
- Article
- Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup-emerging targets to combat antibiotic resistance.Frontiers in chemistry · 2023Review
- Kinetic and Structural Characterization of the First B3 Metallo-β-Lactamase with an Active-Site Glutamic Acid.Antimicrobial agents and chemotherapy · 2021Article
- 2-Mercaptomethyl Thiazolidines (MMTZs) Inhibit All Metallo-β-Lactamase Classes by Maintaining a Conserved Binding Mode.ACS infectious diseases · 2021Article
- Dual Activity BLEG-1 fromInternational journal of molecular sciences · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Mobile Carbapenemase Genes inFrontiers in microbiology · 2021Review
- Structural Insights for Core Scaffold and Substrate Specificity of B1, B2, and B3 Metallo-β-Lactamases.Frontiers in microbiology · 2021Article
- Recent advances in the development of β-lactamase inhibitors.Journal of microbiology (Seoul, Korea) · 2020Review
- Broad spectrum antibiotic-degrading metallo-β-lactamases are phylogenetically diverse.Protein & cell · 2020Article
- Structural Study of Metal Binding and Coordination in Ancient Metallo-β-Lactamase PNGM-1 Variants.International journal of molecular sciences · 2020Article
- Epidemiology of β-Lactamase-Producing Pathogens.Clinical microbiology reviews · 2020Review
- QM/MM investigation of substrate binding of subclass B3 metallo-β-lactamase SMB-1 from Serratia marcescents: insights into catalytic mechanism.Journal of molecular modeling · 2020Article
- 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.Protein science : a publication of the Protein Society · 2020Article
- Shaping Substrate Selectivity in a Broad-Spectrum Metallo-β-Lactamase.Antimicrobial agents and chemotherapy · 2018Article
- Article
- A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.Nature communications · 2017Article
- Crystal structure and kinetic analysis of the class B3 di-zinc metallo-β-lactamase LRA-12 from an Alaskan soil metagenome.PloS one · 2017Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
Metallo-beta-lactamases (MBLs) are broad-spectrum, Zn(II)-dependent lactamases able to confer resistance to virtually every β-lactam antibiotic currently available. The large diversity of active-site structures and metal content among MBLs from different sources has limited the design of a pan-MBL inhibitor. GOB-18 is a divergent MBL from subclass B3 that is expressed by the opportunistic Gram-negative pathogen Elizabethkingia meningoseptica This MBL is atypical, since several residues conserved in B3 enzymes (such as a metal ligand His) are substituted in GOB enzymes. Here, we report the crystal structure of the periplasmic di-Zn(II) form of GOB-18. This enzyme displays a unique active-site structure, with residue Gln116 coordinating the Zn1 ion through its terminal amide moiety, replacing a ubiquitous His residue. This situation contrasts with that of B2 MBLs, where an equivalent His116Asn substitution leads to a di-Zn(II) inactive species. Instead, both the mono- and di-Zn(II) forms of GOB-18 are active against penicillins, cephalosporins, and carbapenems. In silico docking and molecular dynamics simulations indicate that residue Met221 is not involved in substrate binding, in contrast to Ser221, which otherwise is conserved in most B3 enzymes. These distinctive features are conserved in recently reported GOB orthologues in environmental bacteria. These findings provide valuable information for inhibitor design and also posit that GOB enzymes have alternative functions.
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