OXA-66 structure and oligomerisation of OXAAb enzymes

Yuiko Takebayashi; Sarah Henderson; Dimitri Chirgadze; Philip Warburton; Benjamin Evans

doi:10.1099/acmi.0.000412

OXA-66 structure and oligomerisation of OXAAb enzymes

Yuiko Takebayashi, Sarah Henderson, Dimitri Chirgadze, Philip Warburton, Benjamin Evans^*

^*Corresponding author for this work

School of Cellular and Molecular Medicine

Research output: Contribution to journal › Article (Academic Journal) › peer-review

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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
Pages (from-to)	1-7
Journal	Access Microbiology
Volume	4
Issue number	10
DOIs	https://doi.org/10.1099/acmi.0.000412
Publication status	Published - 3 Oct 2022

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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 Sarah Henderson and Dimitri Chirgadze and Philip Warburton and Benjamin Evans",

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T1 - OXA-66 structure and oligomerisation of OXAAb enzymes

AU - Takebayashi, Yuiko

AU - Henderson, Sarah

AU - Chirgadze, Dimitri

AU - Warburton, Philip

AU - Evans, Benjamin

PY - 2022/10/3

Y1 - 2022/10/3

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

M3 - Article (Academic Journal)

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SN - 2516-8290

VL - 4

SP - 1

EP - 7

JO - Access Microbiology

JF - Access Microbiology

IS - 10

ER -

OXA-66 structure and oligomerisation of OXAAb enzymes

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