OXA-66 structure and oligomerisation of OXAAb enzymes

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. ISSN 2516-8290 (In Press)

[thumbnail of Accepted_manuscript]
Preview
PDF (Accepted_manuscript) - Accepted Version
Available under License Creative Commons Attribution No Derivatives.

Download (4MB) | Preview

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
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
Depositing User: LivePure Connector
Date Deposited: 15 Aug 2022 11:30
Last Modified: 12 Sep 2022 00:29
URI: https://ueaeprints.uea.ac.uk/id/eprint/87248
DOI:

Actions (login required)

View Item View Item