ORCID
- Warburton, Philip: 0000-0002-5810-0296
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.
DOI
10.1099/acmi.0.000412
Publication Date
2022-10-03
Publication Title
Access Microbiology
Volume
4
Issue
10
Embargo Period
2022-10-06
Organisational Unit
School of Biomedical Sciences
Recommended Citation
Takebayashi, Y., Henderson, S., Chirgadze, D., Warburton, P., & Evans, B. (2022) 'OXA-66 structure and oligomerisation of OXAAb enzymes', Access Microbiology, 4(10). Available at: https://doi.org/10.1099/acmi.0.000412
