Work

Functional and Structural Characterization of Diverse NfsB Chloramphenicol Reductase Enzymes from Human Pathogens

Year: 2022

Type: article

Abstract: strains to discover that expression of chloramphenicol reductases is sufficient to confer chloramphenicol resistance to Es. coli, confirming that chloramphenicol reductase activity is widespread across this nitroreductase family. By solving the high-resolution crystal structures of active chloramphenicol reductases, we identified residues important for this activity. Our work supports the hypothesis that housekeeping proteins possessing multiple activities can evolve into antibiotic resistance enzymes.

Source: Microbiology Spectrum

DOI: 10.1128/spectrum.00139-22

Authors: Michael W. Mullowney, Natalia I. Maltseva, Michael Endres, Youngchang Kim, Andrzej Joachimiak, Terence S. Crofts

Institutions: Northwestern University, Argonne National Laboratory, University of Chicago

Language: English

Topic: Antibiotic Resistance in Bacteria

Subfield: Molecular Medicine

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: gold

Estimated APC paid: $2,500