Takebayashi, Yuiko, Henderson, Sara R., Chirgadze, Dimitri Y., Warburton, Philip J. and Evans, Benjamin A. ORCID: https://orcid.org/0000-0001-6849-9758 (2022) OXA-66 structure and oligomerisation of OXAAb enzymes. Access Microbiology, 4 (10). ISSN 2516-8290
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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.
Item Type: | Article |
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Additional Information: | Data Summary: The crystal structure of OXA-66 has been deposited in the Protein Data Bank (PDB) with the PDB ID: 6T1H. The coordinate files, diffraction data and validation report can be downloaded from the PDB, DOI: 10.2210/pdb6t1h/pdb. Funding information: The experiments described in this paper were funded by Anglia Ruskin University. SRH was funded by a grant from the Wellcome Trust awarded to BAE (grant reference 213979/Z/18/Z). |
Faculty \ School: | Faculty of Medicine and Health Sciences > Norwich Medical School |
UEA Research Groups: | Faculty of Medicine and Health Sciences > Research Groups > Gastroenterology and Gut Biology Faculty of Medicine and Health Sciences > Research Centres > Metabolic Health Faculty of Medicine and Health Sciences > Research Groups > Pathogen Biology Group |
Depositing User: | LivePure Connector |
Date Deposited: | 15 Aug 2022 11:30 |
Last Modified: | 10 Dec 2024 01:39 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/87248 |
DOI: | 10.1099/acmi.0.000412 |
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