OXA-66 structure and oligomerisation of OXAAb enzymes

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

doi:10.1099/acmi.0.000412

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 language	English
Article number	000412
Journal	Access Microbiology
Volume	4
Issue number	10
Early online date	3 Oct 2022
DOIs	https://doi.org/10.1099/acmi.0.000412
Publication status	Published - Oct 2022

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10.1099/acmi.0.000412Licence: CC BY

Accepted_manuscriptAccepted author manuscript, 4.12 MBLicence: CC BY-ND
acmi000412Final published version, 1.16 MBLicence: CC BY

Cite this

@article{3637102e01364cb6b201a736ba30eba1,

title = "OXA-66 structure and oligomerisation of OXAAb enzymes",

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 {\AA} 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.",

author = "Yuiko Takebayashi and Henderson, {Sara R.} and Chirgadze, {Dimitri Y.} and Warburton, {Philip J.} and Evans, {Benjamin A.}",

note = "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).",

year = "2022",

month = oct,

doi = "10.1099/acmi.0.000412",

language = "English",

volume = "4",

journal = "Access Microbiology",

issn = "2516-8290",

publisher = "Microbiology Society",

number = "10",

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TY - JOUR

T1 - OXA-66 structure and oligomerisation of OXAAb enzymes

AU - Takebayashi, Yuiko

AU - Henderson, Sara R.

AU - Chirgadze, Dimitri Y.

AU - Warburton, Philip J.

AU - Evans, Benjamin A.

N1 - 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).

PY - 2022/10

Y1 - 2022/10

N2 - 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.

AB - 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.

U2 - 10.1099/acmi.0.000412

DO - 10.1099/acmi.0.000412

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JO - Access Microbiology

JF - Access Microbiology

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