OXA-66 structure and oligomerisation of OXAAb enzymes

Yuiko Takebayashi, Sara R. Henderson, Dimitri Y. Chirgadze, Philip J. Warburton, Benjamin A. Evans

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Abstract

The OXA β-lactamases are responsible for hydrolysing β-lactam antibiotics and contribute to the multidrug-resistant phenotype of several major human pathogens. The OXAAb enzymes are intrinsic to Acinetobacter baumannii and can confer resistance to carbapenem antibiotics. Here we determined the structure of the most prevalent OXAAb enzyme, OXA-66. The structure of OXA-66 was solved at a resolution of 2.1 Å and found to be very similar to the structure of OXA-51, the only other OXAAb enzyme that has had its structure solved. Our data contained one molecule per asymmetric unit, and analysis of positions responsible for dimer formation in other OXA enzymes suggest that OXA-66 likely exists as a monomer.
Original languageEnglish
Article number000412
JournalAccess Microbiology
Volume4
Issue number10
Early online date3 Oct 2022
DOIs
Publication statusPublished - Oct 2022

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