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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 OXA enzymes are intrinsic to and can confer resistance to carbapenem antibiotics. Here we determined the structure of the most prevalent OXA 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 OXA 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.

Funding
This study was supported by the:
  • Anglia Ruskin University
    • Principle Award Recipient: PhilipJ Warburton
  • Anglia Ruskin University
    • Principle Award Recipient: BenjaminA Evans
  • Wellcome Trust (Award 213979/Z/18/Z)
    • Principle Award Recipient: BenjaminA Evans
  • This is an open-access article distributed under the terms of the Creative Commons Attribution License. This article was made open access via a Publish and Read agreement between the Microbiology Society and the corresponding author’s institution.
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/content/journal/acmi/10.1099/acmi.0.000412
2022-10-03
2024-05-17
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